DB code: S00366

RLCP classification 3.100.220195.81 : Transfer
CATH domain 3.40.50.1240 : Rossmann fold Catalytic domain
E.C. 5.4.2.1
CSA 1qhf
M-CSA 1qhf
MACiE

CATH domain Related DB codes (homologues)
3.40.50.1240 : Rossmann fold S00365 S00363 D00460 D00514

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P62707 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
BPG-dependent PGAM
PGAM
Phosphoglyceromutase
dPGM
EC 5.4.2.1
NP_415276.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489028.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00300 (His_Phos_1)
[Graphical View]
P0A5R6 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
BPG-dependent PGAM
PGAM
Phosphoglyceromutase
dPGM
EC 5.4.2.1
NP_334917.1 (Protein)
NC_002755.2 (DNA/RNA sequence)
YP_006513819.1 (Protein)
NC_018143.1 (DNA/RNA sequence)
YP_177731.1 (Protein)
NC_000962.3 (DNA/RNA sequence)
PF00300 (His_Phos_1)
[Graphical View]
Q6MWZ7 (Possible phosphoglycerate mutase Gpm2
Phosphoglyceromutase
PGAM) (BPG-dependent PGAM)
YP_006516686.1 (Protein)
NC_018143.1 (DNA/RNA sequence)
YP_177944.1 (Protein)
NC_000962.3 (DNA/RNA sequence)
PF00300 (His_Phos_1)
[Graphical View]
P00950 Phosphoglycerate mutase 1
PGAM 1
EC 5.4.2.1
BPG-dependent PGAM 1
MPGM 1
Phosphoglyceromutase 1
NP_012770.1 (Protein)
NM_001179718.1 (DNA/RNA sequence)
PF00300 (His_Phos_1)
[Graphical View]
P36623 Phosphoglycerate mutase
PGAM
EC 5.4.2.1
BPG-dependent PGAM
MPGM
Phosphoglyceromutase
NP_594889.1 (Protein)
NM_001020318.2 (DNA/RNA sequence)
PF00300 (His_Phos_1)
[Graphical View]

KEGG enzyme name
phosphoglycerate mutase
phosphoglycerate phosphomutase
phosphoglyceromutase
glycerate phosphomutase (diphosphoglycerate cofactor)
monophosphoglycerate mutase
monophosphoglyceromutase
diphosphoglycomutase
diphosphoglycerate mutase
bisphosphoglyceromutase
GriP mutase
MPGM
PGA mutase
PGAM-i
PGAM
PGAM-d
PGM

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P62707 GPMA_ECOLI 2-phospho-D-glycerate = 3-phospho-D-glycerate. Homodimer.
P0A5R6 GPMA_MYCTU 2-phospho-D-glycerate = 3-phospho-D-glycerate.
Q6MWZ7 Q6MWZ7_MYCTU
P00950 PMG1_YEAST 2-phospho-D-glycerate = 3-phospho-D-glycerate. Homotetramer.
P36623 PMGY_SCHPO 2-phospho-D-glycerate = 3-phospho-D-glycerate. Monomer.

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C01159 C00631 C00197 C04262
E.C.
Compound 2,3-Bisphospho-D-glycerate 2-Phospho-D-glycerate 3-Phospho-D-glycerate Protein N(tau)-phospho-L-histidine
Type carboxyl group,phosphate group/phosphate ion carbohydrate,carboxyl group,phosphate group/phosphate ion carbohydrate,carboxyl group,phosphate group/phosphate ion
ChEBI 17720
17835
17794
PubChem 186004
439278
439183
1e58A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Intermediate-bound:HIS_10-NEP
1e59A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:VO3 Unbound Unbound Unbound
1riiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GOL Unbound Unbound
1riiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GOL Unbound Unbound
1riiC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1riiD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GOL Unbound Unbound
2a6pA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GOL-SO4 Unbound Unbound
2a6pB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GOL-SO4 Unbound Unbound
1bq3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:IHP Unbound Unbound Unbound
1bq3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1bq3C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1bq3D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:IHP Unbound Unbound Unbound
1bq4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1bq4B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1bq4C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1bq4D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1qhfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:3PG Unbound
1qhfB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:3PG Unbound
3pgmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:3PG Unbound
4pgmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
4pgmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
4pgmC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
4pgmD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
5pgmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
5pgmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
5pgmC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
5pgmD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
5pgmE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
5pgmF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
5pgmG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
5pgmH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1fztA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P00950, P62707, P36623 & literature [18]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1e58A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 10;GLU 88;ARG 9;ASN 16;ARG 61;HIS 183 HIS 10(Phosphorylation) Modified residue H10-NEP
1e59A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 10;GLU 88;ARG 9;ASN 16;ARG 61;HIS 183 HIS 10(Phosphorylation)
1riiA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 12;GLU 90;ARG 11;ASN 18;ARG 63;HIS 183 HIS 12(Phosphorylation)
1riiB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 12;GLU 90;ARG 11;ASN 18;ARG 63;HIS 183 HIS 12(Phosphorylation)
1riiC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 12;GLU 90;ARG 11;ASN 18;ARG 63;HIS 183 HIS 12(Phosphorylation)
1riiD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 12;GLU 90;ARG 11;ASN 18;ARG 63;HIS 183 HIS 12(Phosphorylation)
2a6pA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 13;GLU 85;ARG 12; ;ARG 64;HIS 147 HIS 13(Phosphorylation)
2a6pB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 13;GLU 85;ARG 12; ;ARG 64;HIS 147 HIS 13(Phosphorylation)
1bq3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
1bq3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
1bq3C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
1bq3D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
1bq4A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
1bq4B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
1bq4C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
1bq4D Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
1qhfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
1qhfB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
3pgmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 179 HIS 8(Phosphorylation)
4pgmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
4pgmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
4pgmC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
4pgmD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
5pgmA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
5pgmB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
5pgmC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
5pgmD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
5pgmE Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
5pgmF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
5pgmG Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
5pgmH Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 8;GLU 86;ARG 7;ASN 14;ARG 59;HIS 181 HIS 8(Phosphorylation)
1fztA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 15;GLU 93;ARG 14;ASN 21;ARG 66;HIS 163 HIS 15(Phosphorylation)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Scheme II, p.741-742
[4]
Fig.3, p.125-128
[14]
p.455-457
[15]
p.1825-1826
[18]
Fig.5, p.1511-1515
[23]
p.1076-1077
[24]
p.1133-1137
[26]
p.82-83

References
[1]
Resource
Comments
Medline ID
PubMed ID 6251799
Journal Biochem Biophys Res Commun
Year 1980
Volume 95
Pages 132-9
Authors Hass LF, Miller KB
Title Human erythrocyte phosphoglycerate mutase: evidence for normal catalysis in the absence of added 2,3-bisphospho-D-glycerate.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 6243955
Journal Biochemistry
Year 1980
Volume 19
Pages 738-43
Authors Blattler WA, Knowles JR
Title Phosphoglycerate mutases: stereochemical course of the phosphoryl group transfers catalyzed by the cofactor-dependent enzyme from rabbit muscle and the cofactor-independent enzyme from wheat germ.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 6115417
Journal Philos Trans R Soc Lond B Biol Sci
Year 1981
Volume 293
Pages 177-89
Authors Sternberg MJ, Cohen FE, Taylor WR, Feldmann RJ
Title Analysis and predication of structural motifs in the glycolytic enzymes.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID 81273329
PubMed ID 6115412
Journal Philos Trans R Soc Lond B Biol Sci
Year 1981
Volume 293
Pages 121-30
Authors Winn SI, Watson HC, Harkins RN, Fothergill LA
Title Structure and activity of phosphoglycerate mutase.
Related PDB 3pgm
Related UniProtKB P00950
[5]
Resource
Comments
Medline ID
PubMed ID 6282653
Journal Fed Proc
Year 1982
Volume 41
Pages 2424-31
Authors Knowles JR
Title Phospho transfer enzymes: lessons from stereochemistry.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 6318807
Journal Biochemistry
Year 1983
Volume 22
Pages 6130-4
Authors Hunt AG, Simplaceanu V, Hong JS, Ho C
Title Phosphorus-31 nuclear magnetic resonance investigation of membrane vesicles from Escherichia coli.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 6331428
Journal Biochem Biophys Res Commun
Year 1984
Volume 121
Pages 826-33
Authors Amato SV, Rose ZB, Liebman MN
Title Macro-structural organization of phosphoglycerate mutase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 6331429
Journal Biochem Biophys Res Commun
Year 1984
Volume 121
Pages 834-41
Authors Rose ZB, Kaklij GS
Title The effects of anions on phosphoglycerate mutase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 1659318
Journal Arch Biochem Biophys
Year 1991
Volume 291
Pages 201-11
Authors Mendz GL
Title Stimulation of mutases and isomerases by vanadium.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8110200
Journal Biochem J
Year 1994
Volume 297
Pages 603-8
Authors Nairn J, Price NC, Fothergill-Gilmore LA, Walker GE, Fothergill JE, Dunbar B
Title The amino acid sequence of the small monomeric phosphoglycerate mutase from the fission yeast Schizosaccharomyces pombe.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 8765231
Journal Biochim Biophys Acta
Year 1996
Volume 1296
Pages 69-75
Authors Nairn J, Price NC, Kelly SM, Rigden D, Fothergill-Gilmore LA, Krell T
Title Phosphoglycerate mutase from Schizosaccharomyces pombe: development of an expression system and characterisation of three histidine mutants of the enzyme.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 9030753
Journal Eur J Biochem
Year 1997
Volume 243
Pages 306-14
Authors Seip S, Lanz R, Gutknecht R, Flukiger K, Erni B
Title The fructose transporter of Bacillus subtilis encoded by the lev operon: backbone assignment and secondary structure of the IIB(Lev) subunit.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 9390410
Journal J Biomol NMR
Year 1997
Volume 10
Pages 309-10
Authors Uhrinova S, Uhrin D, Nairn J, Price NC, Fothergill-Gilmore LA, Barlow PN
Title Backbone assignment of double labelled 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID 98173871
PubMed ID 9512715
Journal J Mol Biol
Year 1998
Volume 276
Pages 449-59
Authors Rigden DJ, Alexeev D, Phillips SE, Fothergill-Gilmore LA
Title The 2.3 A X-ray crystal structure of S. cerevisiae phosphoglycerate mutase.
Related PDB 4pgm
Related UniProtKB P00950
[15]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10531478
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 1822-6
Authors Crowhurst GS, Dalby AR, Isupov MN, Campbell JW, Littlechild JA
Title Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.
Related PDB 1qhf
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 10437801
Journal FEBS Lett
Year 1999
Volume 455
Pages 344-8
Authors Fraser HI, Kvaratskhelia M, White MF
Title The two analogous phosphoglycerate mutases of Escherichia coli.
Related PDB
Related UniProtKB
[17]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10369755
Journal J Mol Biol
Year 1999
Volume 289
Pages 691-9
Authors Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA
Title Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis.
Related PDB 1bq3 1bq4
Related UniProtKB
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10064712
Journal J Mol Biol
Year 1999
Volume 286
Pages 1507-17
Authors Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA
Title Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism.
Related PDB 5pgm
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 11106417
Journal Eur J Biochem
Year 2000
Volume 267
Pages 7065-74
Authors Nairn J, Duncan D, Price NE, Kelly SM, Fothergill-Gilmore LA, Uhrinova S, Barlow PN, Rigden DJ, Price NC
Title Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of the roles of amino acids involved in substrate binding and catalysis.
Related PDB
Related UniProtKB
[20]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11038361
Journal J Biol Chem
Year 2001
Volume 276
Pages 3247-53
Authors Bond CS, White MF, Hunter WN
Title High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase.
Related PDB 1e58
Related UniProtKB P62707
[21]
Resource
Comments NMR, 21 STRUCTURES
Medline ID
PubMed ID 11237600
Journal J Mol Biol
Year 2001
Volume 306
Pages 275-90
Authors Uhrinova S, Uhrin D, Nairn J, Price NC, Fothergill-Gilmore LA, Barlow PN
Title Solution structure and dynamics of an open beta-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe.
Related PDB 1fzt
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 11514674
Journal Protein Sci
Year 2001
Volume 10
Pages 1835-46
Authors Rigden DJ, Bagyan I, Lamani E, Setlow P, Jedrzejas MJ
Title A cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus is actually a broad specificity phosphatase.
Related PDB
Related UniProtKB
[23]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
Medline ID
PubMed ID 11884145
Journal J Mol Biol
Year 2002
Volume 316
Pages 1071-81
Authors Bond CS, White MF, Hunter WN
Title Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex.
Related PDB 1e59
Related UniProtKB P62707
[24]
Resource
Comments
Medline ID
PubMed ID 11827481
Journal J Mol Biol
Year 2002
Volume 315
Pages 1129-43
Authors Rigden DJ, Mello LV, Setlow P, Jedrzejas MJ
Title Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 11951058
Journal Med Sci Monit
Year 2002
Volume 8
Pages BR123-35
Authors Torshin IY
Title Functional maps of the junctions between interglobular contacts and active sites in glycolytic enzymes -- a comparative analysis of the biochemical and structural data.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 12586342
Journal FEBS Lett
Year 2003
Volume 536
Pages 77-84
Authors Rigden DJ
Title Unexpected catalytic site variation in phosphoprotein phosphatase homologues of cofactor-dependent phosphoglycerate mutase.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 15258155
Journal J Biol Chem
Year 2004
Volume 279
Pages 39132-8
Authors Wang Y, Wei Z, Bian Q, Cheng Z, Wan M, Liu L, Gong W
Title Crystal structure of human bisphosphoglycerate mutase.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 15735341
Journal Acta Crystallogr D Biol Crystallogr
Year 2005
Volume 61
Pages 309-15
Authors Muller P, Sawaya MR, Pashkov I, Chan S, Nguyen C, Wu Y, Perry LJ, Eisenberg D
Title The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase.
Related PDB 1rii
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 16672613
Journal J Bacteriol
Year 2006
Volume 188
Pages 3589-99
Authors Watkins HA, Baker EN
Title Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.
Related PDB 2a6p
Related UniProtKB

Comments
This enzyme is homologous to a phosphatase (E.C. 3.1.3.46; S00365 in EzCatDB).
This enzyme catalyzes a kind of intermolecular transfer reaction, which comprises the following steps of the reaction in the double-displacement mechanism.
(a) 2,3-BPG (cofactor) + enzyme => 3-PGA (or 2-PGA) (product) + phosphorylated enzyme
(b) 2-PGA (or 3-PGA) (substrate) + phosphorylated enzyme => 2,3-BPG (cofactor) + enzyme
Accoding to the literature [14], [18], [23], [24] & [26], the reaction mechanism of this enzyme seems to be as follows:
(a) 2,3-BPG (cofactor) + enzyme => 3-PGA (or 2-PGA) (product) + phosphorylated enzyme
(1) Arg59 and His181 modulate the nucleophilicity of His8, keeping His8 unprotonated.
(2) His8 makes a nucleophilic attack on one of the phosphoryl groups of 2,3-BPG, leading to a pentacovalent transition-state.
(3) The transition state seems to be stabilized by Arg7, Asn14, Arg59 and His181, whereas Glu86 acts as a general acid to protonate the leaving hydroxyl group, probably through a water molecule.
(b) 2-PGA (or 3-PGA) (substrate) + phosphorylated enzyme => 2,3-BPG (cofactor) + enzyme
(4) Glu86 now acts as a general base to deprotonate and activate another hydroxyl group of substrate.
(5) The activated acceptor, hydroxyl group, makes a nucleophilic attack on the phosphoryl group on His8, leading to a transition state.
(6) The transition state seems to be stabilized by Arg7, Asn14, Arg59 and His181.

Created Updated
2005-06-14 2015-10-27