EzCatDB: D00005
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DB codeD00005
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
Domain 23.90.110.10 : L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2Catalytic domain
E.C.1.1.1.27
CSA1ldm

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109
3.90.110.10 : L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2D00008,M00171,D00827

Enzyme Name
UniProtKBKEGG

P00344P00343P16115E8ME30Q27743P00341P00339P00336P00342P00338P07195
Protein nameL-lactate dehydrogenaseL-lactate dehydrogenaseL-lactate dehydrogenase
L-lactate dehydrogenaseL-lactate dehydrogenase A chainL-lactate dehydrogenase A chainL-lactate dehydrogenase B chainL-lactate dehydrogenase C chainL-lactate dehydrogenase A chainL-lactate dehydrogenase B chainL-lactate dehydrogenase
lactic acid dehydrogenase
L(+)-nLDH
L-(+)-lactate dehydrogenase
L-lactic dehydrogenase
L-lactic acid dehydrogenase
lactate dehydrogenase
lactate dehydrogenase NAD+-dependent
lactic dehydrogenase
NAD+-lactate dehydrogenase
SynonymsL-LDH
EC 1.1.1.27
L-LDH
EC 1.1.1.27
L-LDH
EC 1.1.1.27
NoneEC 1.1.1.27
LDH-P
LDH-A
EC 1.1.1.27
LDH-M
LDH-A
EC 1.1.1.27
LDH muscle subunit
LDH-M
LDH-B
EC 1.1.1.27
LDH heart subunit
LDH-H
LDH-C
EC 1.1.1.27
LDH testis subunit
LDH-X
LDH-A
EC 1.1.1.27
LDH muscle subunit
LDH-M
Renal carcinoma antigen NY-REN-59
Cell proliferation-inducing gene 19 protein
LDH-B
EC 1.1.1.27
LDH heart subunit
LDH-H
Renal carcinoma antigen NY-REN-46
RefSeq

NP_229663.1 (Protein)
NC_000853.1 (DNA/RNA sequence)
YP_004221049.1 (Protein)
NC_015067.1 (DNA/RNA sequence)



NP_001106758.1 (Protein)
NM_001113287.1 (DNA/RNA sequence)
NP_038608.1 (Protein)
NM_013580.4 (DNA/RNA sequence)
NP_001128711.1 (Protein)
NM_001135239.1 (DNA/RNA sequence)
NP_001158886.1 (Protein)
NM_001165414.1 (DNA/RNA sequence)
NP_001158887.1 (Protein)
NM_001165415.1 (DNA/RNA sequence)
NP_001158888.1 (Protein)
NM_001165416.1 (DNA/RNA sequence)
NP_005557.1 (Protein)
NM_005566.3 (DNA/RNA sequence)
NP_001167568.1 (Protein)
NM_001174097.1 (DNA/RNA sequence)
NP_002291.1 (Protein)
NM_002300.6 (DNA/RNA sequence)
PfamPF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis
MAP00272Cysteine metabolism
MAP00620Pyruvate metabolism
MAP00640Propanoate metabolism

UniProtKB:Accession NumberP00344P00343P16115E8ME30Q27743P00341P00339P00336P00342P00338P07195
Entry nameLDH_BACSTLDH_LACCALDH_THEMALDH2_BIFL2LDH_PLAFDLDHA_SQUACLDHA_PIGLDHB_PIGLDHC_MOUSELDHA_HUMANLDHB_HUMAN
Activity(S)-lactate + NAD(+) = pyruvate + NADH.(S)-lactate + NAD(+) = pyruvate + NADH.(S)-lactate + NAD(+) = pyruvate + NADH.(S)-lactate + NAD(+) = pyruvate + NADH.(S)-lactate + NAD(+) = pyruvate + NADH.(S)-lactate + NAD(+) = pyruvate + NADH.(S)-lactate + NAD(+) = pyruvate + NADH.(S)-lactate + NAD(+) = pyruvate + NADH.(S)-lactate + NAD(+) = pyruvate + NADH.(S)-lactate + NAD(+) = pyruvate + NADH.(S)-lactate + NAD(+) = pyruvate + NADH.
SubunitHomotetramer.Homotetramer.Homotetramer.Homotetramer (By similarity).Homotetramer.Homotetramer.Homotetramer.Homotetramer.Homotetramer.Homotetramer.Homotetramer.
Subcellular locationCytoplasm.Cytoplasm.Cytoplasm.Cytoplasm (By similarity).
Cytoplasm.Cytoplasm.Cytoplasm.Cytoplasm.Cytoplasm.Cytoplasm.
Cofactor











Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00186C00003C00022C00004C00080
Compound(S)-LactateNAD+PyruvateNADHH+
Typecarbohydrate,carboxyl groupamide group,amine group,nucleotidecarbohydrate,carboxyl groupamide group,amine group,nucleotideothers
ChEBI422
15846
32816
16908
15378
PubChem107689
5893
1060
439153
1038
             
1ldbA01UnboundUnboundUnboundUnbound 
1ldnA01UnboundBound:NADUnboundUnbound 
1ldnB01UnboundBound:NADUnboundUnbound 
1ldnC01UnboundBound:NADUnboundUnbound 
1ldnD01UnboundBound:NADUnboundUnbound 
1ldnE01UnboundBound:NADUnboundUnbound 
1ldnF01UnboundBound:NADUnboundUnbound 
1ldnG01UnboundBound:NADUnboundUnbound 
1ldnH01UnboundBound:NADUnboundUnbound 
2ldbA01UnboundBound:NADUnboundUnbound 
1llcA01UnboundUnboundUnboundUnbound 
1a5zA01UnboundBound:NADUnboundUnbound 
1lldA01UnboundBound:NADUnboundUnbound 
1lldB01UnboundBound:NADUnboundUnbound 
1lthR01UnboundBound:NADUnboundUnbound 
1lthT01UnboundBound:NADUnboundUnbound 
1ceqA01UnboundUnboundUnboundUnbound 
1cetA01UnboundUnboundUnboundUnbound 
1ldgA01UnboundBound:NADUnboundUnbound 
1t24A01UnboundBound:NADUnboundUnbound 
1t25A01UnboundUnboundUnboundBound:NAI 
1t26A01UnboundUnboundUnboundBound:NAI 
1t2cA01UnboundUnboundUnboundBound:NAI 
1t2dA01UnboundBound:NADUnboundUnbound 
1t2eA01UnboundUnboundUnboundBound:NAI 
1u4oA01UnboundUnboundUnboundUnbound 
1u4sA01UnboundUnboundUnboundUnbound 
1u5aA01UnboundUnboundUnboundUnbound 
1u5cA01UnboundBound:NADUnboundUnbound 
1xivA01UnboundUnboundUnboundUnbound 
2a94A01UnboundUnboundUnboundAnalogue:AP0 
1ldmA01UnboundBound:NADUnboundUnbound 
3ldhA01UnboundBound:NADUnboundUnbound 
6ldhA01UnboundUnboundUnboundUnbound 
8ldhA01UnboundUnboundUnboundUnbound 
9ldbA01UnboundBound:NADUnboundUnbound 
9ldbB01UnboundBound:NADUnboundUnbound 
9ldtA01UnboundBound:NADUnboundUnbound 
9ldtB01UnboundBound:NADUnboundUnbound 
5ldhA01UnboundAnalogue:LNC(NAD)UnboundUnbound 
2ldxA01UnboundUnboundUnboundUnbound 
1i10A01UnboundUnboundUnboundBound:NAI 
1i10B01UnboundUnboundUnboundBound:NAI 
1i10C01UnboundUnboundUnboundBound:NAI 
1i10D01UnboundUnboundUnboundBound:NAI 
1i10E01UnboundUnboundUnboundBound:NAI 
1i10F01UnboundUnboundUnboundBound:NAI 
1i10G01UnboundUnboundUnboundBound:NAI 
1i10H01UnboundUnboundUnboundBound:NAI 
1i0zA01UnboundUnboundUnboundBound:NAI 
1i0zB01UnboundUnboundUnboundBound:NAI 
1t2fA01UnboundBound:NADUnboundUnbound 
1t2fB01UnboundBound:NADUnboundUnbound 
1t2fC01UnboundBound:NADUnboundUnbound 
1t2fD01UnboundBound:NADUnboundUnbound 
1ldbA02UnboundUnboundUnboundUnbound 
1ldnA02UnboundUnboundAnalogue:OXMUnbound 
1ldnB02UnboundUnboundAnalogue:OXMUnbound 
1ldnC02UnboundUnboundAnalogue:OXMUnbound 
1ldnD02UnboundUnboundAnalogue:OXMUnbound 
1ldnE02UnboundUnboundAnalogue:OXMUnbound 
1ldnF02UnboundUnboundAnalogue:OXMUnbound 
1ldnG02UnboundUnboundAnalogue:OXMUnbound 
1ldnH02UnboundUnboundAnalogue:OXMUnbound 
2ldbA02UnboundUnboundUnboundUnbound 
1llcA02UnboundUnboundUnboundUnbound 
1a5zA02UnboundUnboundAnalogue:OXMUnbound 
1lldA02UnboundUnboundUnboundUnbound 
1lldB02UnboundUnboundUnboundUnbound 
1lthR02UnboundUnboundAnalogue:OXMUnbound 
1lthT02UnboundUnboundUnboundUnbound 
1ceqA02UnboundUnboundUnboundUnbound 
1cetA02UnboundUnboundUnboundUnbound 
1ldgA02UnboundUnboundAnalogue:OXMUnbound 
1t24A02UnboundUnboundAnalogue:OXQUnbound 
1t25A02UnboundUnboundAnalogue:GAGUnbound 
1t26A02UnboundUnboundAnalogue:GBDUnbound 
1t2cA02UnboundUnboundUnboundUnbound 
1t2dA02UnboundUnboundAnalogue:OXLUnbound 
1t2eA02UnboundUnboundAnalogue:OXMUnbound 
1u4oA02UnboundUnboundUnboundUnbound 
1u4sA02UnboundUnboundUnboundUnbound 
1u5aA02UnboundUnboundAnalogue:BIKUnbound 
1u5cA02UnboundUnboundAnalogue:BIKUnbound 
1xivA02UnboundUnboundUnboundUnbound 
2a94A02UnboundUnboundUnboundUnbound 
1ldmA02UnboundUnboundAnalogue:OXMUnbound 
3ldhA02UnboundUnboundBound:PYRUnbound 
6ldhA02UnboundUnboundUnboundUnbound 
8ldhA02Analogue:CIT 1UnboundUnboundUnbound 
9ldbA02UnboundUnboundUnboundUnbound 
9ldbB02UnboundUnboundAnalogue:OXMUnbound 
9ldtA02UnboundUnboundAnalogue:OXMUnbound 
9ldtB02UnboundUnboundAnalogue:OXMUnbound 
5ldhA02Analogue:LNC(S-lactate)UnboundUnboundUnbound 
2ldxA02UnboundUnboundUnboundUnbound 
1i10A02UnboundUnboundAnalogue:OXMUnbound 
1i10B02UnboundUnboundAnalogue:OXMUnbound 
1i10C02UnboundUnboundAnalogue:OXMUnbound 
1i10D02UnboundUnboundAnalogue:OXMUnbound 
1i10E02UnboundUnboundAnalogue:OXMUnbound 
1i10F02UnboundUnboundAnalogue:OXMUnbound 
1i10G02UnboundUnboundAnalogue:OXMUnbound 
1i10H02UnboundUnboundAnalogue:OXMUnbound 
1i0zA02UnboundUnboundAnalogue:OXMUnbound 
1i0zB02UnboundUnboundAnalogue:OXMUnbound 
1t2fA02UnboundUnboundAnalogue:OXQUnbound 
1t2fB02UnboundUnboundAnalogue:OXQUnbound 
1t2fC02UnboundUnboundAnalogue:OXQUnbound 
1t2fD02UnboundUnboundAnalogue:OXQUnbound 

Active-site residues
resource
Swiss-prot;Q27743, P00336, P00339, P00341, P00342, P00344, P00343, P16115, literature [22]
pdbCatalytic residuescomment
          
1ldbA01       
invisible 100-107
1ldnA01ARG 106
 
1ldnB01ARG 106
 
1ldnC01ARG 106
 
1ldnD01ARG 106
 
1ldnE01ARG 106
 
1ldnF01ARG 106
 
1ldnG01ARG 106
 
1ldnH01ARG 106
 
2ldbA01       
invisible 99-106
1llcA01ARG 109
 
1a5zA01ARG 109
 
1lldA01ARG  93
 
1lldB01ARG  93
 
1lthR01ARG  93
 
1lthT01ARG  93
 
1ceqA01ARG 109
 
1cetA01ARG 109
 
1ldgA01ARG 109
 
1t24A01ARG 109
 
1t25A01ARG 109
 
1t26A01ARG 109
 
1t2cA01ARG 109
 
1t2dA01ARG  94
 
1t2eA01ARG 109
 
1u4oA01ARG 109
 
1u4sA01ARG 109
 
1u5aA01ARG 109
 
1u5cA01ARG 109
 
1xivA01ARG 109
 
2a94A01ARG 109
 
1ldmA01ARG 106
 
3ldhA01ARG 109
 
6ldhA01ARG 106
 
8ldhA01ARG 106
 
9ldbA01ARG 109
 
9ldbB01ARG 109
 
9ldtA01ARG 109
 
9ldtB01ARG 109
 
5ldhA01ARG 109
 
2ldxA01ARG 105
 
1i10A01ARG 105
 
1i10B01ARG 105
 
1i10C01ARG 105
 
1i10D01ARG 105
 
1i10E01ARG 105
 
1i10F01ARG 105
 
1i10G01       
invisible 101-106
1i10H01ARG 105
 
1i0zA01ARG 106
 
1i0zB01ARG 106
 
1t2fA01ARG 106
 
1t2fB01ARG 106
 
1t2fC01ARG 106
 
1t2fD01ARG 106
 
1ldbA02ASP 166;ARG 169;HIS 193
 
1ldnA02ASP 166;ARG 169;HIS 193
 
1ldnB02ASP 166;ARG 169;HIS 193
 
1ldnC02ASP 166;ARG 169;HIS 193
 
1ldnD02ASP 166;ARG 169;HIS 193
 
1ldnE02ASP 166;ARG 169;HIS 193
 
1ldnF02ASP 166;ARG 169;HIS 193
 
1ldnG02ASP 166;ARG 169;HIS 193
 
1ldnH02ASP 166;ARG 169;HIS 193
 
2ldbA02ASP 166;ARG 169;HIS 193
 
1llcA02ASP 168;ARG 171;HIS 195
 
1a5zA02ASP 168;ARG 171;HIS 195
 
1lldA02ASP 153;ARG 156;HIS 180
mutant C199S
1lldB02ASP 153;ARG 156;HIS 180
mutant C199S
1lthR02ASP 153;ARG 156;HIS 180
mutant C199S
1lthT02ASP 153;ARG 156;HIS 180
mutant C199S
1ceqA02ASP 168;ARG 171;HIS 195
 
1cetA02ASP 168;ARG 171;HIS 195
 
1ldgA02ASP 168;ARG 171;HIS 195
 
1t24A02ASP 168;ARG 171;HIS 195
 
1t25A02ASP 168;ARG 171;HIS 195
 
1t26A02ASP 168;ARG 171;HIS 195
 
1t2cA02ASP 168;ARG 171;HIS 195
 
1t2dA02ASP 154;ARG 157;HIS 181
 
1t2eA02ASP 168;ARG 171;HIS 195
 
1u4oA02ASP 168;ARG 171;HIS 195
 
1u4sA02ASP 168;ARG 171;HIS 195
 
1u5aA02ASP 168;ARG 171;HIS 195
 
1u5cA02ASP 168;ARG 171;HIS 195
 
1xivA02ASP 168;ARG 171;HIS 195
 
2a94A02ASP 168;ARG 171;HIS 195
 
1ldmA02ASP 166;ARG 169;HIS 193
 
3ldhA02ASP 168;ARG 171;HIS 195
 
6ldhA02ASP 166;ARG 169;HIS 193
 
8ldhA02ASP 166;ARG 169;HIS 193
 
9ldbA02ASP 168;ARG 171;HIS 195
 
9ldbB02ASP 168;ARG 171;HIS 195
 
9ldtA02ASP 168;ARG 171;HIS 195
 
9ldtB02ASP 168;ARG 171;HIS 195
 
5ldhA02ASP 168;ARG 171;HIS 195
 
2ldxA02ASP 165;ARG 168;HIS 192
 
1i10A02ASP 165;ARG 168;HIS 192
 
1i10B02ASP 165;ARG 168;HIS 192
 
1i10C02ASP 165;ARG 168;HIS 192
 
1i10D02ASP 165;ARG 168;HIS 192
 
1i10E02ASP 165;ARG 168;HIS 192
 
1i10F02ASP 165;ARG 168;HIS 192
 
1i10G02ASP 165;ARG 168;HIS 192
 
1i10H02ASP 165;ARG 168;HIS 192
 
1i0zA02ASP 166;ARG 169;HIS 193
 
1i0zB02ASP 166;ARG 169;HIS 193
 
1t2fA02ASP 166;ARG 169;HIS 193
 
1t2fB02ASP 166;ARG 169;HIS 193
 
1t2fC02ASP 166;ARG 169;HIS 193
 
1t2fD02ASP 166;ARG 169;HIS 193
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.2, p.2677-2679
[5]Fig.9, p.303-305
[9]p.462-465
[12]Fig.1, p.178-179
[16]Fig.12, p.1133-1137
[22]Fig. 1, p.228
[23]p.771
[28]p.1355-1358

references
[1]
CommentsATOMIC COORDINATES
PubMed ID4795361
JournalBiochem Biophys Res Commun
Year1973
Volume53
Pages46-51
AuthorsAdams MJ, Ford GC, Liljas A, Rossmann MG
TitleAtomic co-ordinates for dogfish M4 apo-lactate dehydrogenase.
Related UniProtKBP00341
[2]
CommentsX-ray crystallography
PubMed ID940154
JournalJ Mol Biol
Year1976
Volume102
Pages759-79
AuthorsWhite JL, Hackert ML, Buehner M, Adams MJ, Ford GC, Lentz PJ Jr, Smiley IE, Steindel SJ, Rossmann MG
TitleA comparison of the structures of apo dogfish M4 lactate dehydrogenase and its ternary complexes.
Related PDB3ldh
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
PubMed ID197516
JournalProc Natl Acad Sci U S A
Year1977
Volume74
Pages2677-81
AuthorsEventoff W, Rossmann MG, Taylor SS, Torff HJ, Meyer H, Keil W, Kiltz HH
TitleStructural adaptations of lactate dehydrogenase isozymes.
Related UniProtKBP00341
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS)
PubMed ID468772
JournalJ Biol Chem
Year1979
Volume254
Pages7611-20
AuthorsMusick WD, Rossmann MG
TitleThe structure of mouse testicular lactate dehydrogenase isoenzyme C4 at 2.9 A resolution.
Related UniProtKBP00342
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
PubMed ID7338899
JournalJ Mol Biol
Year1981
Volume151
Pages289-307
AuthorsGrau UM, Trommer WE, Rossmann MG
TitleStructure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 A resolution.
Related PDB5ldh
Related UniProtKBP00336
[6]
CommentsX-ray crystallography
PubMed ID6411465
JournalEur J Biochem
Year1983
Volume134
Pages503-11
AuthorsHensel R, Mayr U, Yang CY
TitleThe complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei.
Related PDB1llc
[7]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
JournalActa Crystallogr A
Year1984
Volume40
Pages32-4
AuthorsBuehner M, Hecht HJ
TitleStructure determination of the allosteric L-lactate dehydrogenase from Lactobacillus-casei at 3A resolution.
Related UniProtKBP00343
[8]
CommentsX-ray crystallography
PubMed ID2443489
JournalJ Biol Chem
Year1987
Volume262
Pages13155-62
AuthorsHogrefe HH, Griffith JP, Rossmann MG, Goldberg E
TitleCharacterization of the antigenic sites on the refined 3-A resolution structure of mouse testicular lactate dehydrogenase C4.
Related PDB2ldx
[9]
CommentsX-RAY CRYSTALLOGRAPHY (0.25 ANGSTROMS).
PubMed ID3430615
JournalJ Mol Biol
Year1987
Volume198
Pages445-67
AuthorsAbad-Zapatero C, Griffith JP, Sussman JL, Rossmann MG
TitleRefined crystal structure of dogfish M4 apo-lactate dehydrogenase.
Related PDB1ldm,6ldh,8ldh
Related UniProtKBP00341
[10]
PubMed ID2610514
JournalAppl Biochem Biotechnol
Year1989
Volume22
Pages169-79
AuthorsSimon ES, Plante R, Whitesides GM
TitleD-lactate dehydrogenase. Substrate specificity and use as a catalyst in the synthesis of homochiral 2-hydroxy acids.
[11]
CommentsX-ray crystallography
PubMed ID2330370
JournalProteins
Year1990
Volume7
Pages74-92
AuthorsPiontek K, Chakrabarti P, Schar HP, Rossmann MG, Zuber H
TitleStructure determination and refinement of Bacillus stearothermophilus lactate dehydrogenase.
Related PDB1ldb,2ldb
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
PubMed ID1678537
JournalPhilos Trans R Soc Lond B Biol Sci
Year1991
Volume332
Pages177-84
AuthorsDunn CR, Wilks HM, Halsall DJ, Atkinson T, Clarke AR, Muirhead H, Holbrook JJ
TitleDesign and synthesis of new enzymes based on the lactate dehydrogenase framework.
Related PDB9ldb,9ldt
Related UniProtKBP00339
[13]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
PubMed ID1731077
JournalJ Mol Biol
Year1992
Volume223
Pages317-35
AuthorsWigley DB, Gamblin SJ, Turkenburg JP, Dodson EJ, Piontek K, Muirhead H, Holbrook JJ
TitleStructure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution.
Related PDB1ldn
Related UniProtKBP00344
[14]
PubMed ID1304374
JournalProtein Sci
Year1992
Volume1
Pages892-901
AuthorsCortes A, Emery DC, Halsall DJ, Jackson RM, Clarke AR, Holbrook JJ
TitleCharge balance in the alpha-hydroxyacid dehydrogenase vacuole: an acid test.
[15]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
PubMed ID8450537
JournalJ Mol Biol
Year1993
Volume230
Pages21-7
AuthorsIwata S, Ohta T
TitleMolecular basis of allosteric activation of bacterial L-lactate dehydrogenase.
Related PDB1lld
Related UniProtKBP19869
[16]
PubMed ID8120891
JournalJ Mol Biol
Year1994
Volume1123-4
Pages236(4)
AuthorsGoldberg JD, Yoshida T, Brick P
TitleCrystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 A resolution.
[17]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
PubMed ID7656036
JournalNat Struct Biol
Year1994
Volume1
Pages176-85
AuthorsIwata S, Kamata K, Yoshida S, Minowa T, Ohta T
TitleT and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control.
Related PDB1lth
Related UniProtKBP19869
[18]
PubMed ID8532681
JournalProtein Eng
Year1995
Volume8
Pages565-73
AuthorsPhilippopoulos M, Xiang Y, Lim C
TitleIdentifying the mechanism of protein loop closure: a molecular dynamics simulation of the Bacillus stearothermophilus LDH loop in solution.
[19]
CommentsX-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS)
PubMed ID8901865
JournalNat Struct Biol
Year1996
Volume3
Pages912-5
AuthorsDunn CR, Banfield MJ, Barker JJ, Higham CW, Moreton KM, Turgut-Balik D, Brady RL, Holbrook JJ
TitleThe structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design.
Related PDB1ceq,1ldg
Related UniProtKBQ27743
[20]
PubMed ID9162946
JournalProteins
Year1996
Volume24
Pages450-66
Authorsvan der Spoel D, Vogel HJ, Berendsen HJ
TitleMolecular dynamics simulations of N-terminal peptides from a nucleotide binding protein.
[21]
PubMed ID9017191
JournalBiophys J
Year1997
Volume72
Pages619-26
Authorsvan Beek J, Callender R, Gunner MR
TitleThe contribution of electrostatic and van der Waals interactions to the stereospecificity of the reaction catalyzed by lactate dehydrogenase.
[22]
PubMed ID9329087
JournalProteins
Year1997
Volume29
Pages228-39
AuthorsDafforn TR, Badcoe IG, Sessions RB, el Hawrani AS, Holbrook JJ
TitleCorrelation of the enzyme activities of Bacillus stearothermophilus lactate dehydrogenase on three substrates with the results of molecular dynamics/energy minimization conformational searching.
[23]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
PubMed ID9655830
JournalStructure
Year1998
Volume6
Pages769-81
AuthorsAuerbach G, Ostendorp R, Prade L, Korndorfer I, Dams T, Huber R, Jaenicke R
TitleLactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization.
Related PDB1a5z
Related UniProtKBP16115
[24]
CommentsX-ray crystallography
PubMed ID10187806
JournalJ Biol Chem
Year1999
Volume274
Pages10213-8
AuthorsRead JA, Wilkinson KW, Tranter R, Sessions RB, Brady RL
TitleChloroquine binds in the cofactor binding site of Plasmodium falciparum lactate dehydrogenase.
Related PDB1cet
[25]
PubMed ID10556245
JournalProtein Eng
Year1999
Volume12
Pages851-6
AuthorsHolmberg N, Ryde U, Bulow L
TitleRedesign of the coenzyme specificity in L-lactate dehydrogenase from bacillus stearothermophilus using site-directed mutagenesis and media engineering.
[26]
PubMed ID10951199
JournalEur J Biochem
Year2000
Volume267
Pages5413-20
AuthorsBerr K, Wassenberg D, Lilie H, Behlke J, Jaenicke R
Titleepsilon-crystallin from duck eye lens comparison of its quaternary structure and stability with other lactate dehydrogenases and complex formation with alpha-crystallin.
[27]
PubMed ID11401572
JournalBiochemistry
Year2001
Volume40
Pages7247-52
AuthorsKedzierski P, Moreton K, Clarke AR, Holbrook JJ
TitleThe A245K mutation exposes another stage of the bacterial L-lactate dehydrogenase reaction mechanism.
[28]
PubMed ID11292347
JournalJ Mol Biol
Year2001
Volume307
Pages1351-62
AuthorsLee BI, Chang C, Cho SJ, Eom SH, Kim KK, Yu YG, Suh SW
TitleCrystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases.
[29]
CommentsX-ray crystallography
PubMed ID11276087
JournalProteins
Year2001
Volume43
Pages175-85
AuthorsRead JA, Winter VJ, Eszes CM, Sessions RB, Brady RL
TitleStructural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase.
Related PDB1i0z,1i10
[30]
PubMed ID11807949
JournalProteins
Year2002
Volume46
Pages206-14
AuthorsUchikoba H, Fushinobu S, Wakagi T, Konno M, Taguchi H, Matsuzawa H
TitleCrystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfaces.
[31]
PubMed ID12967707
JournalMol Biochem Parasitol
Year2003
Volume131
Pages1-10
AuthorsWinter VJ, Cameron A, Tranter R, Sessions RB, Brady RL
TitleCrystal structure of Plasmodium berghei lactate dehydrogenase indicates the unique structural differences of these enzymes are shared across the Plasmodium genus.
[32]
PubMed ID15147206
JournalBiochemistry
Year2004
Volume43
Pages6219-29
AuthorsBrown WM, Yowell CA, Hoard A, Vander Jagt TA, Hunsaker LA, Deck LM, Royer RE, Piper RC, Dame JB, Makler MT, Vander Jagt DL
TitleComparative structural analysis and kinetic properties of lactate dehydrogenases from the four species of human malarial parasites.
[33]
PubMed ID15117937
JournalJ Biol Chem
Year2004
Volume279
Pages31429-39
AuthorsCameron A, Read J, Tranter R, Winter VJ, Sessions RB, Brady RL, Vivas L, Easton A, Kendrick H, Croft SL, Barros D, Lavandera JL, Martin JJ, Risco F, Garcia-Ochoa S, Gamo FJ, Sanz L, Leon L, Ruiz JR, Gabarro R, Mallo A, Gomez de las Heras F
TitleIdentification and activity of a series of azole-based compounds with lactate dehydrogenase-directed anti-malarial activity.
Related PDB1t2f,1t24,1t25,1t26,1t2c,1t2d,1t2e
[34]
PubMed ID15978953
JournalMol Biochem Parasitol
Year2005
Volume142
Pages137-48
AuthorsConners R, Schambach F, Read J, Cameron A, Sessions RB, Vivas L, Easton A, Croft SL, Brady RL
TitleMapping the binding site for gossypol-like inhibitors of Plasmodium falciparum lactate dehydrogenase.
Related PDB1u4o,1u4s,1u5a,1u5c,1xiv
[35]
PubMed ID16331982
JournalBiochemistry
Year2005
Volume44
Pages16221-8
AuthorsChaikuad A, Fairweather V, Conners R, Joseph-Horne T, Turgut-Balik D, Brady RL
TitleStructure of lactate dehydrogenase from Plasmodium vivax: complexes with NADH and APADH.
Related PDB2a94

comments
This enzyme belongs to the LDH famiyl in the LDH/MDH superfamily.

createdupdated
2004-12-012012-06-25


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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