DB code: S00225

RLCP classification 8.131.42001.6 : Isomerization
8.113.42001.5 : Isomerization
CATH domain 3.20.20.70 : TIM Barrel Catalytic domain
E.C. 5.3.1.1
CSA 1tph 1hti
M-CSA 1tph 1hti
MACiE M0324

CATH domain Related DB codes (homologues)
3.20.20.70 : TIM Barrel S00215 S00217 S00218 S00219 S00532 S00198 S00220 S00745 S00537 S00538 S00539 S00826 S00841 S00235 S00239 S00240 S00243 S00244 S00199 S00200 S00201 S00221 S00222 S00847 S00224 S00226 D00014 D00029 M00141 T00015 T00239 D00664 D00665 D00804 D00863 T00089

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
P00943 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
P00940 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
NP_990782.1 (Protein)
NM_205451.1 (DNA/RNA sequence)
P0A858 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
NP_418354.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491532.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
P62002 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
NP_579649.1 (Protein)
NC_003413.1 (DNA/RNA sequence)
P62003 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
P48499 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
Q07412 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
P60174 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
NP_000356.1 (Protein)
NM_000365.5 (DNA/RNA sequence)
NP_001152759.1 (Protein)
NM_001159287.1 (DNA/RNA sequence)
NP_001244955.1 (Protein)
NM_001258026.1 (DNA/RNA sequence)
P60175 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
NP_001065250.1 (Protein)
NM_001071782.1 (DNA/RNA sequence)
P04789 Triosephosphate isomerase, glycosomal
TIM
Triose-phosphate isomerase
EC 5.3.1.1
PF00121 (TIM)
[Graphical View]
P52270 Triosephosphate isomerase, glycosomal
TIM
Triose-phosphate isomerase
EC 5.3.1.1
PF00121 (TIM)
[Graphical View]
P50921 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
P00942 Triosephosphate isomerase
TIM
EC 5.3.1.1
Triose-phosphate isomerase
PF00121 (TIM)
[Graphical View]
NP_010335.1 (Protein)
NM_001180358.1 (DNA/RNA sequence)

KEGG enzyme name
triose-phosphate isomerase
phosphotriose isomerase
triose phosphoisomerase
triose phosphate mutase
D-glyceraldehyde-3-phosphate ketol-isomerase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00943 TPIS_BACST D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer. Cytoplasm (Probable).
P00940 TPIS_CHICK D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer.
P0A858 TPIS_ECOLI D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer. Cytoplasm (Probable).
P62002 TPIS_PYRFU D-glyceraldehyde 3-phosphate = glycerone phosphate. Homotetramer (By similarity). Cytoplasm (Probable).
P62003 TPIS_PYRWO D-glyceraldehyde 3-phosphate = glycerone phosphate. Homotetramer. Cytoplasm (Probable).
P48499 TPIS_LEIME D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer. Cytoplasm. Glycosome.
Q07412 TPIS_PLAFA D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer.
P60174 TPIS_HUMAN D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer.
P60175 TPIS_PANTR D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer (By similarity).
P04789 TPIS_TRYBB D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer. Glycosome.
P52270 TPIS_TRYCR D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer. Glycosome.
P50921 TPIS_VIBMA D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer. Cytoplasm (Probable).
P00942 TPIS_YEAST D-glyceraldehyde 3-phosphate = glycerone phosphate. Homodimer.

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis
MAP00031 Inositol metabolism
MAP00051 Fructose and mannose metabolism
MAP00710 Carbon fixation in photosynthetic organisms

Compound table
Substrates Products Intermediates
KEGG-id C00118 C00111 I00178
E.C.
Compound D-Glyceraldehyde 3-phosphate Glycerone phosphate Enediol form of glycerone phosphate
Type carbohydrate,phosphate group/phosphate ion carbohydrate,phosphate group/phosphate ion
ChEBI 29052
16108
PubChem 439168
668
1ag1O Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ag1T Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1amkA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1aw1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1aw1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1aw1D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1aw1E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1aw1G Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1aw1H Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1aw1J Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1aw1K Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1aw2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1aw2B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1aw2D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1aw2E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1aw2G Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1aw2H Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1aw2J Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1aw2K Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1btmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1btmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1ci1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ci1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1dkwA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1dkwB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1hg3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:3PP
1hg3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:3PP
1hg3C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:3PP
1hg3D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:3PP
1hg3E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:3PP
1hg3F Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:3PP
1hg3G Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:3PP
1hg3H Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:3PP
1htiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1htiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1i45A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1i45B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1if2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:129 Unbound Unbound
1iigA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1iigB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:3PP
1iihA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1iihB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:3PG Unbound Unbound
1kv5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1kv5B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1lyxA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1lzoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1lzoB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1lzoC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1lzoD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1m7oA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:3PG Unbound Unbound
1m7oB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:3PG Unbound Unbound
1m7pA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:G3H Unbound Unbound
1m7pB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:G3H Unbound Unbound
1ml1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1ml1C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1ml1E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1ml1G Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1ml1I Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1ml1K Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1mssA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1mssB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1n55A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1neyA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:13P Unbound
1neyB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:13P Unbound
1nf0A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:13P Unbound
1nf0B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:13P Unbound
1o5xA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:3PY-PO3
1o5xB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:2PG
1qdsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1spqA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1spqB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1sq7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1sq7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ssdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ssdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ssgA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1ssgB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1su5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1su5B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1suxA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1suxB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1sw0A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1sw0B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1sw3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1sw3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1sw7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1sw7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1tcdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tcdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tmhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tmhB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tmhC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tmhD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tpb1 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tpb2 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tpc1 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tpc2 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tpdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tpdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tpeA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tpfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tpfB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tph1 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tph2 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tpuA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tpuB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tpvA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tpvB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tpwA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1tpwB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1trdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1trdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1treA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1treB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1triA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1tsiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:4PB Unbound
1tsiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ttiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
1ttjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
1vgaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1vgaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1vgaC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1vgaD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1woaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:G2H Unbound Unbound
1woaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:G2H Unbound Unbound
1woaC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:G2H Unbound Unbound
1woaD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:G2H Unbound Unbound
1wobA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1wobB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1wobC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1wobD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ydvA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ydvB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ypiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1ypiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
2btmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
2btmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
2ypiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
2ypiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Transition-state-analogue:PGA
3timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
3timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
3ypiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
3ypiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
4timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
4timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Intermediate-analogue:2PG
5timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
5timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
6timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
6timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:G3P Unbound Unbound
7timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
7timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PGH Unbound
8timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
8timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [42], [58], [76] & [102]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ag1O Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1ag1T Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1amkA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1aw1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw1D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw1E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw1G Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw1H Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw1J Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw1K Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw2B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw2D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw2E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw2G Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw2H Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw2J Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1aw2K Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 9;LYS 11;HIS 97;GLU 169
1btmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 8;LYS 10;HIS 94;GLU 166
1btmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 8;LYS 10;HIS 94;GLU 166
1ci1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 168
1ci1B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 168
1dkwA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1dkwB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1hg3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 144
1hg3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 144
1hg3C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 144
1hg3D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 144
1hg3E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 144
1hg3F Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 144
1hg3G Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 144
1hg3H Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 144
1htiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165
1htiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165
1i45A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 FTR 168 mutant W90Y, W157F, W168FTR
1i45B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 FTR 168 mutant W90Y, W157F, W168FTR
1if2A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167 mutant E65Q
1iigA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1iigB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 311;LYS 313;HIS 395;GLU 467
1iihA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1iihB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 311;LYS 313;HIS 395;GLU 467
1kv5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167 mutant R191S
1kv5B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167 mutant R191S
1lyxA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1lzoA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1lzoB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1lzoC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1lzoD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1m7oA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1m7oB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1m7pA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1m7pB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1ml1A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1ml1C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1ml1E Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1ml1G Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1ml1I Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1ml1K Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1mssA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167 mutant F45S, V46S, 68-72 GNADALAS
1mssB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167 mutant F45S, V46S, 68-72 GNADALAS
1n55A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167 mutant E65Q
1neyA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 FTR 168 mutant W90Y, W157F, W168FTR
1neyB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 FTR 168 mutant W90Y, W157F, W168FTR
1nf0A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 FTR 168 mutant W90Y, W157F, W168FTR
1nf0B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 FTR 168 mutant W90Y, W157F, W168FTR
1o5xA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant A163V
1o5xB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant A163V
1qdsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167 mutant E65Q
1spqA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant A176K
1spqB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant A176K
1sq7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174L, T175W
1sq7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174L, T175W
1ssdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174Y, T175S, A176L
1ssdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174Y, T175S, A176L
1ssgA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174Y, T175S, A176L
1ssgB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174Y, T175S, A176L
1su5A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174N, T175P, A176N
1su5B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174N, T175P, A176N
1suxA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 168
1suxB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 168
1sw0A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174L, T175W
1sw0B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174L, T175W
1sw3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant T175V
1sw3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant T175V
1sw7A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174N, T175S, A176S
1sw7B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant K174N, T175S, A176S
1tcdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 168
1tcdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 12;LYS 14;HIS 96;GLU 168
1timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165
1timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165
1tmhA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 97;GLU 169 mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242
1tmhB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 97;GLU 169 mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242
1tmhC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 97;GLU 169 mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242
1tmhD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 97;GLU 169 mutant P227H, I229V, A232F, A241P, A243E, A245V, V246D, V248I, K249N, deletion D242
1tpb1 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95; mutant E165D
1tpb2 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95; mutant E165D
1tpc1 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95; mutant S96P, E165D
1tpc2 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95; mutant S96P, E165D
1tpdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1tpdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1tpeA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1tpfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1tpfB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1tph1 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165
1tph2 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165
1tpuA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13; ;GLU 165 mutant H95N
1tpuB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13; ;GLU 165 mutant H95N
1tpvA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13; ;GLU 165 mutant H95N, S96P
1tpvB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13; ;GLU 165 mutant H95N, S96P
1tpwA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant S96P
1tpwB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165 mutant S96P
1trdA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1trdB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1treA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 97;GLU 169
1treB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 97;GLU 169
1triA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11; ;HIS 95;GLU 167 mutant 68-82 GNADALAS, invisible K13
1tsiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1tsiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
1ttiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167 mutant I68G, A69N, K70A, S71D, P81A, A100W, deletion 73-79
1ttjA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11; ;HIS 95;GLU 167 mutant F45S, V46S, invisible K13
1vgaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant W168F
1vgaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant W168F
1vgaC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant W168F
1vgaD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant W168F
1woaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant A163V, W168F
1woaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant A163V, W168F
1woaC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant A163V, W168F
1woaD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant A163V, W168F
1wobA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant A163V, W168F
1wobB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant A163V, W168F
1wobC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant A163V, W168F
1wobD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165 mutant A163V, W168F
1ydvA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1ydvB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1ypiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
1ypiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
2btmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 8;LYS 10;HIS 94;GLU 166
2btmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 8;LYS 10;HIS 94;GLU 166
2ypiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
2ypiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
3timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
3timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
3ypiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12; ;GLU 165 mutant H95Q
3ypiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12; ;GLU 165 mutant H95Q
4timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
4timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
5timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
5timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
6timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
6timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 167
7timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
7timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 10;LYS 12;HIS 95;GLU 165
8timA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165
8timB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 11;LYS 13;HIS 95;GLU 165

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Fig.1, p.159-161, p.168-170
[4]
Fig.1, p.604, p.607-612
[5]
p.120
[7]
Fig.1
[9]
Fig.1, Fig.4
[10]
Scheme I, p.3187
[11]
Fig.1, p.678
[12]
Scheme I
[13]
Fig.1, Fig.2, Fig.4
[14]
Scheme I, Scheme II, p.3016-3017
[15]
Fig.1, Fig.2
[21]
FIG.1
[27]
Scheme I
[28]
Fig.3, p.241-243
[29]
Fig.1
[33]
Fig.1
[34]
Fig.1
[35]
Fig.1
[40]
Fig.3, p.314
[42]
Fig.2
[43]
Fig.1
[44]
[45]
Fig.1
[50]
Fig.1
[53]
Fig.1
[54]
Fig.1
[56]
Fig.1, p.232-234
[58]
Scheme 1, Scheme 3, Fig.8
[67]
Fig.1, p.4395-4396
[69]
SCHEME 1
[76]
Fig.1, p.5194
[78]
Fig.1
[87]
Scheme 1, Fig.1
[88]
Scheme 1
[90]
SCHEME I, SCHEME II, Fig.6
[93]
FIG.1
[94]
FIG.1, p.52468-52469
[95]
Scheme 1, p.47
[97]
Fig.1, Fig.3, p.52-54
[99]
[102]
Fig.1, p.229-230

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND REVISION.
Medline ID 75175220
PubMed ID 1134550
Journal Nature
Year 1975
Volume 255
Pages 609-14
Authors Banner DW, Bloomer AC, Petsko GA, Phillips DC, Pogson CI, Wilson IA, Corran PH, Furth AJ, Milman JD, Offord RE, Priddle JD, Waley SG
Title Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data.
Related PDB
Related UniProtKB P00940
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY.
Medline ID 77044751
PubMed ID 985462
Journal Biochem Biophys Res Commun
Year 1976
Volume 72
Pages 146-55
Authors Banner DW, Bloomer A, Petsko GA, Phillips DC, Wilson IA
Title Atomic coordinates for triose phosphate isomerase from chicken muscle.
Related PDB 1tim
Related UniProtKB P00940
[3]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 6115415
Journal Philos Trans R Soc Lond B Biol Sci
Year 1981
Volume 293
Pages 159-71
Authors Alber T, Banner DW, Bloomer AC, Petsko GA, Phillips D, Rivers PS, Wilson IA
Title On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase.
Related PDB 1ml1
Related UniProtKB
[4]
Resource
Comments REVIEW.
Medline ID 88295752
PubMed ID 3331346
Journal Cold Spring Harb Symp Quant Biol
Year 1987
Volume 52
Pages 603-13
Authors Alber TC, Davenport RC Jr, Giammona DA, Lolis E, Petsko GA, Ringe D
Title Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?
Related PDB
Related UniProtKB P00942
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID 88118904
PubMed ID 3430602
Journal J Mol Biol
Year 1987
Volume 198
Pages 109-21
Authors Wierenga RK, Kalk KH, Hol WG
Title Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 A resolution.
Related PDB
Related UniProtKB P04789
[6]
Resource
Comments
Medline ID
PubMed ID 2260979
Journal Biochem Biophys Res Commun
Year 1990
Volume 173
Pages 736-40
Authors Schnackerz KD, Kuan TK, Goux WJ, Gracy RW
Title Phosphorus-31 nuclear magnetic resonance spectroscopy reveals two conformational forms of chloroacetol phosphate-bound triosephosphate isomerase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 2361134
Journal Biochemistry
Year 1990
Volume 29
Pages 4099-108
Authors Blacklow SC, Knowles JR
Title How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases.
Related PDB
Related UniProtKB
[8]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID 90373768
PubMed ID 2204417
Journal Biochemistry
Year 1990
Volume 29
Pages 6609-18
Authors Lolis E, Alber T, Davenport RC, Rose D, Hartman FC, Petsko GA
Title Structure of yeast triosephosphate isomerase at 1.9-A resolution.
Related PDB 1ypi
Related UniProtKB P00942
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE.
Medline ID 90373769
PubMed ID 2204418
Journal Biochemistry
Year 1990
Volume 29
Pages 6619-25
Authors Lolis E, Petsko GA
Title Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
Related PDB 2ypi
Related UniProtKB P00942
[10]
Resource
Comments
Medline ID
PubMed ID 2185832
Journal Biochemistry
Year 1990
Volume 29
Pages 3186-94
Authors Pompliano DL, Peyman A, Knowles JR
Title Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 2217142
Journal Protein Eng
Year 1990
Volume 3
Pages 677-90
Authors Daggett V, Kollman PA
Title Molecular dynamics simulations of active site mutants of triosephosphate isomerase.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 1883832
Journal Biochemistry
Year 1991
Volume 30
Pages 8470-6
Authors Blacklow SC, Liu KD, Knowles JR
Title Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase.
Related PDB
Related UniProtKB
[13]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2043623
Journal Biochemistry
Year 1991
Volume 30
Pages 5821-6
Authors Davenport RC, Bash PA, Seaton BA, Karplus M, Petsko GA, Ringe D
Title Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway.
Related PDB 7tim
Related UniProtKB
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2007138
Journal Biochemistry
Year 1991
Volume 30
Pages 3011-9
Authors Komives EA, Chang LC, Lolis E, Tilton RF, Petsko GA, Knowles JR
Title Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95.
Related PDB 3ypi
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 2069953
Journal Biochemistry
Year 1991
Volume 30
Pages 6948-56
Authors Lodi PJ, Knowles JR
Title Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implications.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 1814699
Journal Ciba Found Symp
Year 1991
Volume 161
Pages 91-103; discussion 103-7
Authors Kollman PA, Daggett V, Dang LX
Title The application of computational methods to the study of enzyme catalysis by triose-phosphate isomerase and stabilities of variants of bacteriophage T4 lysozyme.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 2065677
Journal Eur J Biochem
Year 1991
Volume 199
Pages 231-8
Authors Schnackerz KD, Gracy RW
Title Probing the catalytic sites of triosephosphate isomerase by 31P-NMR with reversibly and irreversibly binding substrate analogues.
Related PDB
Related UniProtKB
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2040290
Journal Eur J Biochem
Year 1991
Volume 198
Pages 53-7
Authors Verlinde CL, Noble ME, Kalk KH, Groendijk H, Wierenga RK, Hol WG
Title Anion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate.
Related PDB 1ag1
Related UniProtKB
[19]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1895291
Journal J Med Chem
Year 1991
Volume 34
Pages 2709-18
Authors Noble ME, Verlinde CL, Groendijk H, Kalk KH, Wierenga RK, Hol WG
Title Crystallographic and molecular modeling studies on trypanosomal triosephosphate isomerase: a critical assessment of the predicted and observed structures of the complex with 2-phosphoglycerate.
Related PDB 4tim
Related UniProtKB
[20]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
Medline ID 91350193
PubMed ID 1880808
Journal J Mol Biol
Year 1991
Volume 220
Pages 995-1015
Authors Wierenga RK, Noble ME, Vriend G, Nauche S, Hol WG
Title Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex.
Related PDB 5tim
Related UniProtKB P04789
[21]
Resource
Comments
Medline ID
PubMed ID 2005961
Journal Nature
Year 1991
Volume 350
Pages 121-4
Authors Knowles JR
Title Enzyme catalysis: not different, just better.
Related PDB
Related UniProtKB
[22]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2062828
Journal Proteins
Year 1991
Volume 10
Pages 50-69
Authors Noble ME, Wierenga RK, Lambeir AM, Opperdoes FR, Thunnissen AM, Kalk KH, Groendijk H, Hol WG
Title The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
Related PDB 6tim 1iig 1iih
Related UniProtKB
[23]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH 2-P-GLYCOLATE.
Medline ID
PubMed ID 2062827
Journal Proteins
Year 1991
Volume 10
Pages 33-49
Authors Wierenga RK, Noble ME, Postma JP, Groendijk H, Kalk KH, Hol WG, Opperdoes FR
Title The crystal structure of the "open" and the "closed" conformation of the flexible loop of trypanosomal triosephosphate isomerase.
Related PDB 3tim
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 1536574
Journal Arch Biochem Biophys
Year 1992
Volume 293
Pages 382-90
Authors Sun AQ, Yuksel KU, Gracy RW
Title Relationship between the catalytic center and the primary degradation site of triosephosphate isomerase: effects of active site modification and deamidation.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 1586170
Journal Arch Biochem Biophys
Year 1992
Volume 295
Pages 421-8
Authors Sun AQ, Yuksel KU, Rao GS, Gracy RW
Title Effects of active site modification and reversible dissociation on the secondary structure of triosephosphate isomerase.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 1390633
Journal Biochemistry
Year 1992
Volume 31
Pages 8488-94
Authors Sampson NS, Knowles JR
Title Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 1390632
Journal Biochemistry
Year 1992
Volume 31
Pages 8482-7
Authors Sampson NS, Knowles JR
Title Segmental movement: definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 1290934
Journal Faraday Discuss
Year 1992
Volume (93)
Pages 239-48
Authors Karplus M, Evanseck JD, Joseph D, Bash PA, Field MJ
Title Simulation analysis of triose phosphate isomerase: conformational transition and catalysis.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 1628747
Journal FEBS Lett
Year 1992
Volume 306
Pages 80-4
Authors Hennig M, Schlesier B, Dauter Z, Pfeffer S, Betzel C, Hohne WE, Wilson KS
Title A TIM barrel protein without enzymatic activity? Crystal-structure of narbonin at 1.8 A resolution.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 1639191
Journal FEBS Lett
Year 1992
Volume 307
Pages 34-9
Authors Wierenga RK, Borchert TV, Noble ME
Title Crystallographic binding studies with triosephosphate isomerases: conformational changes induced by substrate and substrate-analogues.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 1400336
Journal J Biol Chem
Year 1992
Volume 267
Pages 20168-74
Authors Sun AQ, Yuksel KU, Gracy RW
Title Interactions between the catalytic centers and subunit interface of triosephosphate isomerase probed by refolding, active site modification, and subunit exchange.
Related PDB
Related UniProtKB
[32]
Resource
Comments X-RAY CRYSTALLOGRAPHY.
Medline ID 92235847
PubMed ID 1569570
Journal J Mol Biol
Year 1992
Volume 224
Pages 1115-26
Authors Wierenga RK, Noble ME, Davenport RC
Title Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase.
Related PDB
Related UniProtKB P00940 P00942 P04789
[33]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1304889
Journal Protein Sci
Year 1992
Volume 1
Pages 1578-84
Authors Verlinde CL, Witmans CJ, Pijning T, Kalk KH, Hol WG, Callens M, Opperdoes FR
Title Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformation.
Related PDB 1tsi
Related UniProtKB
[34]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID
PubMed ID 15299515
Journal Acta Crystallogr D Biol Crystallogr
Year 1993
Volume 49(Pt 4)
Pages 403-17
Authors Noble ME.M, Zeelen JP, Wierenga RK, Mainfroid V, Goraj K, Gohimont A-C, Martial JA
Title Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution.
Related PDB 1tre
Related UniProtKB P0A858
[35]
Resource
Comments
Medline ID
PubMed ID 8476863
Journal Biochemistry
Year 1993
Volume 32
Pages 4338-43
Authors Lodi PJ, Knowles JR
Title Direct evidence for the exploitation of an alpha-helix in the catalytic mechanism of triosephosphate isomerase.
Related PDB
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 8431552
Journal Biophys J
Year 1993
Volume 64
Pages 9-15
Authors Wade RC, Davis ME, Luty BA, Madura JD, McCammon JA
Title Gating of the active site of triose phosphate isomerase: Brownian dynamics simulations of flexible peptide loops in the enzyme.
Related PDB
Related UniProtKB
[37]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND REVISION TO 203.
Medline ID 93170303
PubMed ID 8436128
Journal Eur J Biochem
Year 1993
Volume 211
Pages 703-10
Authors Borchert TV, Pratt K, Zeelen JP, Callens M, Noble ME, Opperdoes FR, Michels PA, Wierenga RK
Title Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant.
Related PDB
Related UniProtKB P04789
[38]
Resource
Comments
Medline ID
PubMed ID 8262920
Journal J Biol Chem
Year 1993
Volume 268
Pages 26872-8
Authors Sun AQ, Yuksel KU, Gracy RW
Title Limited proteolysis of triose-phosphate isomerase and characterization of the catalytically active peptide complex.
Related PDB
Related UniProtKB
[39]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID 94143343
PubMed ID 8309937
Journal Protein Eng
Year 1993
Volume 6
Pages 893-900
Authors Mainfroid V, Goraj K, Rentier-Delrue F, Houbrechts A, Loiseau A, Gohimont AC, Noble ME, Borchert TV, Wierenga RK, Martial JA
Title Replacing the (beta alpha)-unit 8 of E.coli TIM with its chicken homologue leads to a stable and active hybrid enzyme.
Related PDB
Related UniProtKB P0A858
[40]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8356028
Journal Proteins
Year 1993
Volume 16
Pages 311-26
Authors Noble ME, Zeelen JP, Wierenga RK
Title Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism.
Related PDB 1tpd 1trd
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 8204630
Journal Biochemistry
Year 1994
Volume 33
Pages 6960-5
Authors Garza-Ramos G, Tuena de Gomez-Puyou M, Gomez-Puyou A, Yuksel KU, Gracy RW
Title Deamidation of triosephosphate isomerase in reverse micelles: effects of water on catalysis and molecular wear and tear.
Related PDB
Related UniProtKB
[42]
Resource
Comments
Medline ID
PubMed ID 8130194
Journal Biochemistry
Year 1994
Volume 33
Pages 2815-23
Authors Joseph-McCarthy D, Lolis E, Komives EA, Petsko GA
Title Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site.
Related PDB
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 7907502
Journal Biochemistry
Year 1994
Volume 33
Pages 2824-9
Authors Joseph-McCarthy D, Rost LE, Komives EA, Petsko GA
Title Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic base glutamic acid 165 is changed to aspartic acid.
Related PDB
Related UniProtKB
[44]
Resource
Comments
Medline ID
PubMed ID 8130193
Journal Biochemistry
Year 1994
Volume 33
Pages 2809-14
Authors Lodi PJ, Chang LC, Knowles JR, Komives EA
Title Triosephosphate isomerase requires a positively charged active site: the role of lysine-12.
Related PDB
Related UniProtKB
[45]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID 94176473
PubMed ID 8130195
Journal Biochemistry
Year 1994
Volume 33
Pages 2830-7
Authors Zhang Z, Sugio S, Komives EA, Liu KD, Knowles JR, Petsko GA, Ringe D
Title Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution.
Related PDB 1tph
Related UniProtKB P00940
[46]
Resource
Comments
Medline ID
PubMed ID 7906272
Journal J Biol Chem
Year 1994
Volume 269
Pages 5005-8
Authors Yuksel KU, Sun AQ, Gracy RW, Schnackerz KD
Title The hinged lid of yeast triose-phosphate isomerase. Determination of the energy barrier between the two conformations.
Related PDB
Related UniProtKB
[47]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7809033
Journal Protein Eng
Year 1994
Volume 7
Pages 945-51
Authors Kishan R, Zeelen JP, Noble ME, Borchert TV, Mainfroid V, Goraj K, Martial JA, Wierenga RK
Title Modular mutagenesis of a TIM-barrel enzyme: the crystal structure of a chimeric E. coli TIM having the eighth beta alpha-unit replaced by the equivalent unit of chicken TIM.
Related PDB 1tmh
Related UniProtKB
[48]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8061607
Journal Protein Sci
Year 1994
Volume 3
Pages 779-87
Authors Kishan KV, Zeelen JP, Noble ME, Borchert TV, Wierenga RK
Title Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms.
Related PDB 1tpe 1tpf
Related UniProtKB
[49]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID 94339841
PubMed ID 8061610
Journal Protein Sci
Year 1994
Volume 3
Pages 810-21
Authors Mande SC, Mainfroid V, Kalk KH, Goraj K, Martial JA, Hol WG
Title Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme.
Related PDB 1hti
Related UniProtKB P60174
[50]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7577950
Journal Biochemistry
Year 1995
Volume 34
Pages 13612-21
Authors Komives EA, Lougheed JC, Liu K, Sugio S, Zhang Z, Petsko GA, Ringe D
Title The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules.
Related PDB 1tpb 1tpc
Related UniProtKB
[51]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID 96164392
PubMed ID 8580851
Journal Protein Sci
Year 1995
Volume 4
Pages 2594-604
Authors Delboni LF, Mande SC, Rentier-Delrue F, Mainfroid V, Turley S, Vellieux FM, Martial JA, Hol WG
Title Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions.
Related PDB 1btm
Related UniProtKB P00943
[52]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANTS.
Medline ID 96000857
PubMed ID 8591044
Journal Structure
Year 1995
Volume 3
Pages 669-79
Authors Borchert TV, Kishan KV, Zeelen JP, Schliebs W, Thanki N, Abagyan R, Jaenicke R, Wierenga RK
Title Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8.
Related PDB 1tri 1tti 1ttj
Related UniProtKB P04789
[53]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8952501
Journal Biochemistry
Year 1996
Volume 35
Pages 15474-84
Authors Komives EA, Lougheed JC, Zhang Z, Sugio S, Narayana N, Xuong NH, Petsko GA, Ringe D
Title The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase.
Related PDB 1tpu 1tpv
Related UniProtKB
[54]
Resource
Comments
Medline ID
PubMed ID 8626554
Journal J Biol Chem
Year 1996
Volume 271
Pages 10010-6
Authors Aqvist J, Fothergill M
Title Computer simulation of the triosephosphate isomerase catalyzed reaction.
Related PDB
Related UniProtKB
[55]
Resource
Comments
Medline ID
PubMed ID 8745400
Journal Protein Sci
Year 1996
Volume 5
Pages 229-39
Authors Schliebs W, Thanki N, Eritja R, Wierenga R
Title Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies.
Related PDB
Related UniProtKB
[56]
Resource
Comments
Medline ID
PubMed ID 8811738
Journal Proteins
Year 1996
Volume 25
Pages 225-36
Authors Perakyla M, Pakkanen TA
Title Ab initio models for receptor-ligand interactions in proteins. 4. Model assembly study of the catalytic mechanism of triosephosphate isomerase.
Related PDB
Related UniProtKB
[57]
Resource
Comments
Medline ID
PubMed ID 9126273
Journal Arch Biochem Biophys
Year 1997
Volume 340
Pages 27-35
Authors Talent JM, Zvaigzne AI, Agrawal N, Gracy RW
Title Effect of active-site modification on the terminal marking deamidation of triosephosphate isomerase.
Related PDB
Related UniProtKB
[58]
Resource
Comments
Medline ID
PubMed ID 9398185
Journal Biochemistry
Year 1997
Volume 36
Pages 14661-75
Authors Harris TK, Abeygunawardana C, Mildvan AS
Title NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase.
Related PDB
Related UniProtKB
[59]
Resource
Comments
Medline ID
PubMed ID 9245397
Journal Biochemistry
Year 1997
Volume 36
Pages 9655-62
Authors Schliebs W, Thanki N, Jaenicke R, Wierenga RK
Title A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability.
Related PDB
Related UniProtKB
[60]
Resource
Comments
Medline ID
PubMed ID 9089815
Journal Protein Eng
Year 1997
Volume 10
Pages 159-67
Authors Thanki N, Zeelen JP, Mathieu M, Jaenicke R, Abagyan RA, Wierenga RK, Schliebs W
Title Protein engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop.
Related PDB
Related UniProtKB
[61]
Resource
Comments
Medline ID
PubMed ID 9144796
Journal Proteins
Year 1997
Volume 28
Pages 109-16
Authors Kobayashi N, Yamato T, Go N
Title Mechanical property of a TIM-barrel protein.
Related PDB
Related UniProtKB
[62]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF PGK, AND REVISIONS.
Medline ID 98046096
PubMed ID 9384563
Journal Structure
Year 1997
Volume 5
Pages 1475-83
Authors Auerbach G, Huber R, Grattinger M, Zaiss K, Schurig H, Jaenicke R, Jacob U
Title Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability.
Related PDB
Related UniProtKB P36204
[63]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID 97410385
PubMed ID 9261072
Journal Structure
Year 1997
Volume 5
Pages 751-61
Authors Velanker SS, Ray SS, Gokhale RS, Suma S, Balaram H, Balaram P, Murthy MR
Title Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design.
Related PDB 1ydv
Related UniProtKB Q07412
[64]
Resource
Comments NUCLEOTIDE SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Medline ID
PubMed ID 9442062
Journal J Biol Chem
Year 1998
Volume 273
Pages 2199-206
Authors Alvarez M, Zeelen JP, Mainfroid V, Rentier-Delrue F, Martial JA, Wyns L, Wierenga RK, Maes D
Title Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
Related PDB 1aw1 1aw2
Related UniProtKB P50921
[65]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
Medline ID 98437380
PubMed ID 9761683
Journal J Mol Biol
Year 1998
Volume 283
Pages 193-203
Authors Maldonado E, Soriano-Garcia M, Moreno A, Cabrera N, Garza-Ramos G, de Gomez-Puyou M, Gomez-Puyou A, Perez-Montfort R
Title Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes.
Related PDB 1tcd
Related UniProtKB P52270
[66]
Resource
Comments
Medline ID
PubMed ID 10194326
Journal Biochemistry
Year 1999
Volume 38
Pages 4114-20
Authors Perez-Montfort R, Garza-Ramos G, Alcantara GH, Reyes-Vivas H, Gao XG, Maldonado E, de Gomez-Puyou MT, Gomez-Puyou A
Title Derivatization of the interface cysteine of triosephosphate isomerase from Trypanosoma brucei and Trypanosoma cruzi as probe of the interrelationship between the catalytic sites and the dimer interface.
Related PDB
Related UniProtKB
[67]
Resource
Comments
Medline ID
PubMed ID 10194358
Journal Biochemistry
Year 1999
Volume 38
Pages 4389-97
Authors Zhang Z, Komives EA, Sugio S, Blacklow SC, Narayana N, Xuong NH, Stock AM, Petsko GA, Ringe D
Title The role of water in the catalytic efficiency of triosephosphate isomerase.
Related PDB
Related UniProtKB
[68]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID 99315861
PubMed ID 10383424
Journal J Biol Chem
Year 1999
Volume 274
Pages 19181-7
Authors Alvarez M, Wouters J, Maes D, Mainfroid V, Rentier-Delrue F, Wyns L, Depiereux E, Martial JA
Title Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures.
Related PDB 2btm
Related UniProtKB P00943
[69]
Resource
Comments
Medline ID
PubMed ID 10507008
Journal Methods Enzymol
Year 1999
Volume 308
Pages 246-76
Authors Shan SO, Herschlag D
Title Hydrogen bonding in enzymatic catalysis: analysis of energetic contributions.
Related PDB
Related UniProtKB
[70]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID 99398662
PubMed ID 10468562
Journal Proc Natl Acad Sci U S A
Year 1999
Volume 96
Pages 10062-7
Authors Gao XG, Maldonado E, Perez-Montfort R, Garza-Ramos G, de Gomez-Puyou MT, Gomez-Puyou A, Rodriguez-Romero A
Title Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane.
Related PDB 1ci1
Related UniProtKB P52270
[71]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).
Medline ID 99249704
PubMed ID 10235625
Journal Protein Eng
Year 1999
Volume 12
Pages 243-50
Authors Williams JC, Zeelen JP, Neubauer G, Vriend G, Backmann J, Michels PA, Lambeir AM, Wierenga RK
Title Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power.
Related PDB 1amk
Related UniProtKB P48499
[72]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF TIM.
Medline ID 20058648
PubMed ID 10591103
Journal Proteins
Year 1999
Volume 37
Pages 441-53
Authors Maes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, Thi MH, Backmann J, Martial JA, Wyns L, Jaenicke R, Wierenga RK
Title The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures.
Related PDB 1b9b
Related UniProtKB P36204
[73]
Resource
Comments
Medline ID
PubMed ID 10591103
Journal Proteins
Year 1999
Volume 37
Pages 441-53
Authors Maes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, Thi MH, Backmann J, Martial JA, Wyns L, Jaenicke R, Wierenga RK
Title The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures.
Related PDB
Related UniProtKB
[74]
Resource
Comments
Medline ID
PubMed ID 10957646
Journal Acta Crystallogr D Biol Crystallogr
Year 2000
Volume 56
Pages 1201-3
Authors Wouters J, Maes D
Title Identification of a potential metal cation-pi binding site in the structure of a thermophilic Bacillus stearothermophilus triosephosphate isomerase mutant.
Related PDB
Related UniProtKB
[75]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10785370
Journal Eur J Biochem
Year 2000
Volume 267
Pages 2516-24
Authors Lambeir AM, Backmann J, Ruiz-Sanz J, Filimonov V, Nielsen JE, Kursula I, Norledge BV, Wierenga RK
Title The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase.
Related PDB 1qds
Related UniProtKB
[76]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11589711
Journal Eur J Biochem
Year 2001
Volume 268
Pages 5189-96
Authors Kursula I, Partanen S, Lambeir AM, Antonov DM, Augustyns K, Wierenga RK
Title Structural determinants for ligand binding and catalysis of triosephosphate isomerase.
Related PDB 1if2
Related UniProtKB
[77]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11419952
Journal J Mol Biol
Year 2001
Volume 310
Pages 271-80
Authors Rozovsky S, Jogl G, Tong L, McDermott AE
Title Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics.
Related PDB 1i45
Related UniProtKB
[78]
Resource
Comments
Medline ID
PubMed ID 11419951
Journal J Mol Biol
Year 2001
Volume 310
Pages 259-70
Authors Rozovsky S, McDermott AE
Title The time scale of the catalytic loop motion in triosephosphate isomerase.
Related PDB
Related UniProtKB
[79]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11243785
Journal J Mol Biol
Year 2001
Volume 306
Pages 745-57
Authors Walden H, Bell GS, Russell RJ, Siebers B, Hensel R, Taylor GL
Title Tiny TIM: a small, tetrameric, hyperthermostable triosephosphate isomerase.
Related PDB 1hg3
Related UniProtKB P62003
[80]
Resource
Comments
Medline ID
PubMed ID 11286559
Journal J Mol Biol
Year 2001
Volume 307
Pages 1103-12
Authors Xiang J, Sun J, Sampson NS
Title The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase.
Related PDB
Related UniProtKB
[81]
Resource
Comments
Medline ID
PubMed ID 11342710
Journal Protein Eng
Year 2001
Volume 14
Pages 149-55
Authors Saab-Rincon G, Juarez VR, Osuna J, Sanchez F, Soberon X
Title Different strategies to recover the activity of monomeric triosephosphate isomerase by directed evolution.
Related PDB
Related UniProtKB
[82]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11151009
Journal Proteins
Year 2001
Volume 42
Pages 383-9
Authors Norledge BV, Lambeir AM, Abagyan RA, Rottmann A, Fernandez AM, Filimonov VV, Peter MG, Wierenga RK
Title Modeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8) of triosephosphate isomerase: toward a new substrate specificity.
Related PDB 1dkw
Related UniProtKB
[83]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12454456
Journal Acta Crystallogr D Biol Crystallogr
Year 2002
Volume 58
Pages 1992-2000
Authors Parthasarathy S, Balaram H, Balaram P, Murthy MR
Title Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state.
Related PDB 1m7o 1m7p
Related UniProtKB
[84]
Resource
Comments
Medline ID
PubMed ID 11914068
Journal Biochemistry
Year 2002
Volume 41
Pages 4230-8
Authors Hernandez-Alcantara G, Garza-Ramos G, Hernandez GM, Gomez-Puyou A, Perez-Montfort R
Title Catalysis and stability of triosephosphate isomerase from Trypanosoma brucei with different residues at position 14 of the dimer interface. Characterization of a catalytically competent monomeric enzyme.
Related PDB
Related UniProtKB
[85]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12403619
Journal Biochemistry
Year 2002
Volume 41
Pages 13178-88
Authors Parthasarathy S, Ravindra G, Balaram H, Balaram P, Murthy MR
Title Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state.
Related PDB 1lyx 1lzo
Related UniProtKB
[86]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11997014
Journal FEBS Lett
Year 2002
Volume 518
Pages 39-42
Authors Kursula I, Partanen S, Lambeir AM, Wierenga RK
Title The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis.
Related PDB 1kv5
Related UniProtKB
[87]
Resource
Comments
Medline ID
PubMed ID 11902900
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 3093-124
Authors Cui Q, Karplus M
Title Quantum mechanics/molecular mechanics studies of triosephosphate isomerase-catalyzed reactions: effect of geometry and tunneling on proton-transfer rate constants.
Related PDB
Related UniProtKB
[88]
Resource
Comments
Medline ID
PubMed ID 12475328
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 14871-8
Authors Zhang X, Harrison DH, Cui Q
Title Functional specificities of methylglyoxal synthase and triosephosphate isomerase: a combined QM/MM analysis.
Related PDB
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[89]
Resource
Comments
Medline ID
PubMed ID 12185208
Journal J Biol Chem
Year 2002
Volume 277
Pages 30968-75
Authors Silverman JA, Harbury PB
Title Rapid mapping of protein structure, interactions, and ligand binding by misincorporation proton-alkyl exchange.
Related PDB
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[90]
Resource
Comments
Medline ID
PubMed ID 14631822
Journal Adv Protein Chem
Year 2003
Volume 66
Pages 315-72
Authors Cui Q, Karplus M
Title Catalysis and specificity in enzymes: a study of triosephosphate isomerase and comparison with methyl glyoxal synthase.
Related PDB
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[91]
Resource
Comments
Medline ID
PubMed ID 12472469
Journal Biochem J
Year 2003
Volume 370
Pages 785-92
Authors Najera H, Costas M, Fernandez-Velasco DA
Title Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme.
Related PDB
Related UniProtKB
[92]
Resource
Comments
Medline ID
PubMed ID 12627960
Journal Biochemistry
Year 2003
Volume 42
Pages 2941-51
Authors Desamero R, Rozovsky S, Zhadin N, McDermott A, Callender R
Title Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation.
Related PDB
Related UniProtKB
[93]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12522213
Journal J Biol Chem
Year 2003
Volume 278
Pages 9544-51
Authors Kursula I, Wierenga RK
Title Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution.
Related PDB 1n55
Related UniProtKB
[94]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 14563846
Journal J Biol Chem
Year 2003
Volume 278
Pages 52461-70
Authors Parthasarathy S, Eaazhisai K, Balaram H, Balaram P, Murthy MR
Title Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolution.
Related PDB 1o5x
Related UniProtKB
[95]
Resource
Comments
Medline ID
PubMed ID 12483674
Journal J Comput Chem
Year 2003
Volume 24
Pages 46-56
Authors Alagona G, Ghio C, Kollman PA
Title The intramolecular mechanism for the second proton transfer in triosephosphate isomerase (TIM): a QM/FE approach.
Related PDB
Related UniProtKB
[96]
Resource
Comments
Medline ID
PubMed ID 14643664
Journal J Mol Biol
Year 2003
Volume 334
Pages 1023-41
Authors Aparicio R, Ferreira ST, Polikarpov I
Title Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity.
Related PDB
Related UniProtKB
[97]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12509510
Journal Proc Natl Acad Sci U S A
Year 2003
Volume 100
Pages 50-5
Authors Jogl G, Rozovsky S, McDermott AE, Tong L
Title Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.
Related PDB 1ney 1nf0
Related UniProtKB
[98]
Resource
Comments
Medline ID
PubMed ID 15023076
Journal Biochemistry
Year 2004
Volume 43
Pages 3255-63
Authors Gonzalez-Mondragon E, Zubillaga RA, Saavedra E, Chanez-Cardenas ME, Perez-Montfort R, Hernandez-Arana A
Title Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability.
Related PDB
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[99]
Resource
Comments
Medline ID
PubMed ID 15350130
Journal Biochemistry
Year 2004
Volume 43
Pages 11436-45
Authors Xiang J, Jung JY, Sampson NS
Title Entropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase.
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[100]
Resource
Comments
Medline ID
PubMed ID 15324804
Journal Chem Biol
Year 2004
Volume 11
Pages 1037-42
Authors Tousignant A, Pelletier JN
Title Protein motions promote catalysis.
Related PDB
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[101]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 15465054
Journal J Mol Biol
Year 2004
Volume 343
Pages 671-84
Authors Eaazhisai K, Balaram H, Balaram P, Murthy MR
Title Structures of unliganded and inhibitor complexes of W168F, a Loop6 hinge mutant of Plasmodium falciparum triosephosphate isomerase: observation of an intermediate position of loop6.
Related PDB 1vga 1woa 1wob
Related UniProtKB
[102]
Resource
Comments
Medline ID
PubMed ID 15001364
Journal J Mol Biol
Year 2004
Volume 337
Pages 227-39
Authors Guallar V, Jacobson M, McDermott A, Friesner RA
Title Computational modeling of the catalytic reaction in triosephosphate isomerase.
Related PDB
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[103]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 15321726
Journal J Mol Biol
Year 2004
Volume 341
Pages 1355-1365
Authors Tellez-Valencia A, Olivares-Illana V, Hernandez-Santoyo A, Perez-Montfort R, Costas M, Rodriguez-Romero A, Lopez-Calahorra F, Tuena de Gomez-Puyou M, Gomez-Puyou A
Title Inactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface
Related PDB 1sux
Related UniProtKB
[104]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 15166315
Journal Protein Eng Des Sel
Year 2004
Volume 17
Pages 375-82
Authors Kursula I, Salin M, Sun J, Norledge BV, Haapalainen AM, Sampson NS, Wierenga RK
Title Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase.
Related PDB 1spq 1sq7 1ssd 1ssg 1su5 1sw0 1sw3 1sw7
Related UniProtKB
[105]
Resource
Comments
Medline ID
PubMed ID 15103619
Journal Proteins
Year 2004
Volume 55
Pages 548-57
Authors Shukla A, Guptasarma P
Title Folding of beta/alpha-unit scrambled forms of S. cerevisiae triosephosphate isomerase: Evidence for autonomy of substructure formation and plasticity of hydrophobic and hydrogen bonding interactions in core of (beta/alpha)8-barrel.
Related PDB
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[106]
Resource
Comments
Medline ID
PubMed ID 15707966
Journal Biochem Biophys Res Commun
Year 2005
Volume 328
Pages 922-8
Authors Espinoza-Fonseca LM, Trujillo-Ferrara JG
Title Structural considerations for the rational design of selective anti-trypanosomal agents: the role of the aromatic clusters at the interface of triosephosphate isomerase dimer.
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Comments
According to the literature [4], [13], [14], [15], [58], [90], [94], [95] & [102], there have been three possible mechanisms proposed to date, as follows:
(1) Glu165 (of 1ypi) acts as a general acid-base to transfer a (pro-R) proton from C1 to C2 (of substrate), whereas His95 acts as a general acid-base or proton shuttle to transfer a proton from O1 to O2.
(2) Intramolecular proton transfer from O1 to O2.
(3) Glu165 acts as a general acid-base to transfer a (pro-R) proton from C1 to O2 (of substrate), and then transfers a proton from O1 to C2.
According to the literature, as His95 is neutral, which rarely acts as a general base. Moreover, His95 may disturb the intramolecular proton transfer (see [102]. Thus, the mechanism (3) is most likely.
According to the literature [42], [58], [76] & [102], this enzyme catalyzes two successive isomerizations (or shifts of double-bond).
(A) Isomerization; Shift of double-bond from carbonyl group to adjacent C=C.
(A1) Glu165 acts as as a general base to deprotonate the C1 atom of substrate (G3P), which leads to the formation of an enodilate intermediate with double-bond between the C1 and C2 atoms. Here, His95 and Lys12 stabilize the negative charge on the enediolate (or the O2 atom).
(A2) Glu165 acts as a general acid to protonate the O1 atom, leading to the enediol intermediate (I00178).
(B) Isomerization; Shift of double-bond from C=C to carbonyl group.
(B1) Glu165 acts as a general base to deprotonate the O1 hydroxyl atom, leading to the enediolate intermediate. His95 and Asn10 stabilize the negative charge on the O1 atom.
(B2) Glu165 acts as a general acid to protonate the C2 atom, giving the product (GP).

Created Updated
2005-05-11 2014-07-08