DB code: D00005

CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
3.90.110.10 : L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2 Catalytic domain
E.C. 1.1.1.27
CSA 1ldm
M-CSA 1ldm
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 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 2 D00008 M00171 D00827

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
P00343 L-lactate dehydrogenase
L-LDH
EC 1.1.1.27
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
P00344 L-lactate dehydrogenase
L-LDH
EC 1.1.1.27
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
P16115 L-lactate dehydrogenase
L-LDH
EC 1.1.1.27
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
NP_229663.1 (Protein)
NC_000853.1 (DNA/RNA sequence)
E8ME30
None PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
YP_004221049.1 (Protein)
NC_015067.1 (DNA/RNA sequence)
Q27743 L-lactate dehydrogenase
EC 1.1.1.27
LDH-P
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
P00341 L-lactate dehydrogenase A chain
LDH-A
EC 1.1.1.27
LDH-M
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
P00339 L-lactate dehydrogenase A chain
LDH-A
EC 1.1.1.27
LDH muscle subunit
LDH-M
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
P00336 L-lactate dehydrogenase B chain
LDH-B
EC 1.1.1.27
LDH heart subunit
LDH-H
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
NP_001106758.1 (Protein)
NM_001113287.1 (DNA/RNA sequence)
P00342 L-lactate dehydrogenase C chain
LDH-C
EC 1.1.1.27
LDH testis subunit
LDH-X
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
NP_038608.1 (Protein)
NM_013580.4 (DNA/RNA sequence)
P00338 L-lactate dehydrogenase A chain
LDH-A
EC 1.1.1.27
LDH muscle subunit
LDH-M
Renal carcinoma antigen NY-REN-59
Cell proliferation-inducing gene 19 protein
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
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)
P07195 L-lactate dehydrogenase B chain
LDH-B
EC 1.1.1.27
LDH heart subunit
LDH-H
Renal carcinoma antigen NY-REN-46
PF02866 (Ldh_1_C)
PF00056 (Ldh_1_N)
[Graphical View]
NP_001167568.1 (Protein)
NM_001174097.1 (DNA/RNA sequence)
NP_002291.1 (Protein)
NM_002300.6 (DNA/RNA sequence)

KEGG enzyme name
L-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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00344 LDH_BACST (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer. Cytoplasm.
P00343 LDH_LACCA (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer. Cytoplasm.
P16115 LDH_THEMA (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer. Cytoplasm.
E8ME30 LDH2_BIFL2 (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer (By similarity). Cytoplasm (By similarity).
Q27743 LDH_PLAFD (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer.
P00341 LDHA_SQUAC (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer. Cytoplasm.
P00339 LDHA_PIG (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer. Cytoplasm.
P00336 LDHB_PIG (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer. Cytoplasm.
P00342 LDHC_MOUSE (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer. Cytoplasm.
P00338 LDHA_HUMAN (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer. Cytoplasm.
P07195 LDHB_HUMAN (S)-lactate + NAD(+) = pyruvate + NADH. Homotetramer. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis
MAP00272 Cysteine metabolism
MAP00620 Pyruvate metabolism
MAP00640 Propanoate metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00186 C00003 C00022 C00004 C00080
E.C.
Compound (S)-Lactate NAD+ Pyruvate NADH H+
Type carbohydrate,carboxyl group amide group,amine group,nucleotide carbohydrate,carboxyl group amide group,amine group,nucleotide others
ChEBI 422
422
15846
15846
32816
32816
16908
16908
15378
15378
PubChem 107689
107689
5893
5893
1060
1060
439153
439153
1038
1038
1ldbA01 Unbound Unbound Unbound Unbound
1ldnA01 Unbound Bound:NAD Unbound Unbound
1ldnB01 Unbound Bound:NAD Unbound Unbound
1ldnC01 Unbound Bound:NAD Unbound Unbound
1ldnD01 Unbound Bound:NAD Unbound Unbound
1ldnE01 Unbound Bound:NAD Unbound Unbound
1ldnF01 Unbound Bound:NAD Unbound Unbound
1ldnG01 Unbound Bound:NAD Unbound Unbound
1ldnH01 Unbound Bound:NAD Unbound Unbound
2ldbA01 Unbound Bound:NAD Unbound Unbound
1llcA01 Unbound Unbound Unbound Unbound
1a5zA01 Unbound Bound:NAD Unbound Unbound
1lldA01 Unbound Bound:NAD Unbound Unbound
1lldB01 Unbound Bound:NAD Unbound Unbound
1lthR01 Unbound Bound:NAD Unbound Unbound
1lthT01 Unbound Bound:NAD Unbound Unbound
1ceqA01 Unbound Unbound Unbound Unbound
1cetA01 Unbound Unbound Unbound Unbound
1ldgA01 Unbound Bound:NAD Unbound Unbound
1t24A01 Unbound Bound:NAD Unbound Unbound
1t25A01 Unbound Unbound Unbound Unbound
1t26A01 Unbound Unbound Unbound Bound:NAI
1t2cA01 Unbound Unbound Unbound Bound:NAI
1t2dA01 Unbound Bound:NAD Unbound Bound:NAI
1t2eA01 Unbound Unbound Unbound Unbound
1u4oA01 Unbound Unbound Unbound Bound:NAI
1u4sA01 Unbound Unbound Unbound Unbound
1u5aA01 Unbound Unbound Unbound Unbound
1u5cA01 Unbound Bound:NAD Unbound Unbound
1xivA01 Unbound Unbound Unbound Unbound
2a94A01 Unbound Unbound Unbound Unbound
1ldmA01 Unbound Bound:NAD Unbound Analogue:AP0
3ldhA01 Unbound Bound:NAD Unbound Unbound
6ldhA01 Unbound Unbound Unbound Unbound
8ldhA01 Unbound Unbound Unbound Unbound
9ldbA01 Unbound Bound:NAD Unbound Unbound
9ldbB01 Unbound Bound:NAD Unbound Unbound
9ldtA01 Unbound Bound:NAD Unbound Unbound
9ldtB01 Unbound Bound:NAD Unbound Unbound
5ldhA01 Unbound Analogue:LNC(NAD) Unbound Unbound
2ldxA01 Unbound Unbound Unbound Unbound
1i10A01 Unbound Unbound Unbound Unbound
1i10B01 Unbound Unbound Unbound Bound:NAI
1i10C01 Unbound Unbound Unbound Bound:NAI
1i10D01 Unbound Unbound Unbound Bound:NAI
1i10E01 Unbound Unbound Unbound Bound:NAI
1i10F01 Unbound Unbound Unbound Bound:NAI
1i10G01 Unbound Unbound Unbound Bound:NAI
1i10H01 Unbound Unbound Unbound Bound:NAI
1i0zA01 Unbound Unbound Unbound Bound:NAI
1i0zB01 Unbound Unbound Unbound Bound:NAI
1t2fA01 Unbound Bound:NAD Unbound Bound:NAI
1t2fB01 Unbound Bound:NAD Unbound Unbound
1t2fC01 Unbound Bound:NAD Unbound Unbound
1t2fD01 Unbound Bound:NAD Unbound Unbound
1ldbA02 Unbound Unbound Unbound Unbound
1ldnA02 Unbound Unbound Analogue:OXM Unbound
1ldnB02 Unbound Unbound Analogue:OXM Unbound
1ldnC02 Unbound Unbound Analogue:OXM Unbound
1ldnD02 Unbound Unbound Analogue:OXM Unbound
1ldnE02 Unbound Unbound Analogue:OXM Unbound
1ldnF02 Unbound Unbound Analogue:OXM Unbound
1ldnG02 Unbound Unbound Analogue:OXM Unbound
1ldnH02 Unbound Unbound Analogue:OXM Unbound
2ldbA02 Unbound Unbound Unbound Unbound
1llcA02 Unbound Unbound Unbound Unbound
1a5zA02 Unbound Unbound Analogue:OXM Unbound
1lldA02 Unbound Unbound Unbound Unbound
1lldB02 Unbound Unbound Unbound Unbound
1lthR02 Unbound Unbound Analogue:OXM Unbound
1lthT02 Unbound Unbound Unbound Unbound
1ceqA02 Unbound Unbound Unbound Unbound
1cetA02 Unbound Unbound Unbound Unbound
1ldgA02 Unbound Unbound Analogue:OXM Unbound
1t24A02 Unbound Unbound Analogue:OXQ Unbound
1t25A02 Unbound Unbound Analogue:GAG Unbound
1t26A02 Unbound Unbound Analogue:GBD Unbound
1t2cA02 Unbound Unbound Unbound Unbound
1t2dA02 Unbound Unbound Analogue:OXL Unbound
1t2eA02 Unbound Unbound Analogue:OXM Unbound
1u4oA02 Unbound Unbound Unbound Unbound
1u4sA02 Unbound Unbound Unbound Unbound
1u5aA02 Unbound Unbound Analogue:BIK Unbound
1u5cA02 Unbound Unbound Analogue:BIK Unbound
1xivA02 Unbound Unbound Unbound Unbound
2a94A02 Unbound Unbound Unbound Unbound
1ldmA02 Unbound Unbound Analogue:OXM Unbound
3ldhA02 Unbound Unbound Bound:PYR Unbound
6ldhA02 Unbound Unbound Unbound Unbound
8ldhA02 Analogue:CIT_1 Unbound Unbound Unbound
9ldbA02 Unbound Unbound Unbound Unbound
9ldbB02 Unbound Unbound Analogue:OXM Unbound
9ldtA02 Unbound Unbound Analogue:OXM Unbound
9ldtB02 Unbound Unbound Analogue:OXM Unbound
5ldhA02 Analogue:LNC(S-lactate) Unbound Unbound Unbound
2ldxA02 Unbound Unbound Unbound Unbound
1i10A02 Unbound Unbound Analogue:OXM Unbound
1i10B02 Unbound Unbound Analogue:OXM Unbound
1i10C02 Unbound Unbound Analogue:OXM Unbound
1i10D02 Unbound Unbound Analogue:OXM Unbound
1i10E02 Unbound Unbound Analogue:OXM Unbound
1i10F02 Unbound Unbound Analogue:OXM Unbound
1i10G02 Unbound Unbound Analogue:OXM Unbound
1i10H02 Unbound Unbound Analogue:OXM Unbound
1i0zA02 Unbound Unbound Analogue:OXM Unbound
1i0zB02 Unbound Unbound Analogue:OXM Unbound
1t2fA02 Unbound Unbound Analogue:OXQ Unbound
1t2fB02 Unbound Unbound Analogue:OXQ Unbound
1t2fC02 Unbound Unbound Analogue:OXQ Unbound
1t2fD02 Unbound Unbound Analogue:OXQ Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;Q27743, P00336, P00339, P00341, P00342, P00344, P00343, P16115, literature [22]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ldbA01 invisible 100-107
1ldnA01 ARG 106
1ldnB01 ARG 106
1ldnC01 ARG 106
1ldnD01 ARG 106
1ldnE01 ARG 106
1ldnF01 ARG 106
1ldnG01 ARG 106
1ldnH01 ARG 106
2ldbA01 invisible 99-106
1llcA01 ARG 109
1a5zA01 ARG 109
1lldA01 ARG 93
1lldB01 ARG 93
1lthR01 ARG 93
1lthT01 ARG 93
1ceqA01 ARG 109
1cetA01 ARG 109
1ldgA01 ARG 109
1t24A01 ARG 109
1t25A01 ARG 109
1t26A01 ARG 109
1t2cA01 ARG 109
1t2dA01 ARG 94
1t2eA01 ARG 109
1u4oA01 ARG 109
1u4sA01 ARG 109
1u5aA01 ARG 109
1u5cA01 ARG 109
1xivA01 ARG 109
2a94A01 ARG 109
1ldmA01 ARG 106
3ldhA01 ARG 109
6ldhA01 ARG 106
8ldhA01 ARG 106
9ldbA01 ARG 109
9ldbB01 ARG 109
9ldtA01 ARG 109
9ldtB01 ARG 109
5ldhA01 ARG 109
2ldxA01 ARG 105
1i10A01 ARG 105
1i10B01 ARG 105
1i10C01 ARG 105
1i10D01 ARG 105
1i10E01 ARG 105
1i10F01 ARG 105
1i10G01 invisible 101-106
1i10H01 ARG 105
1i0zA01 ARG 106
1i0zB01 ARG 106
1t2fA01 ARG 106
1t2fB01 ARG 106
1t2fC01 ARG 106
1t2fD01 ARG 106
1ldbA02 ASP 166;ARG 169;HIS 193
1ldnA02 ASP 166;ARG 169;HIS 193
1ldnB02 ASP 166;ARG 169;HIS 193
1ldnC02 ASP 166;ARG 169;HIS 193
1ldnD02 ASP 166;ARG 169;HIS 193
1ldnE02 ASP 166;ARG 169;HIS 193
1ldnF02 ASP 166;ARG 169;HIS 193
1ldnG02 ASP 166;ARG 169;HIS 193
1ldnH02 ASP 166;ARG 169;HIS 193
2ldbA02 ASP 166;ARG 169;HIS 193
1llcA02 ASP 168;ARG 171;HIS 195
1a5zA02 ASP 168;ARG 171;HIS 195
1lldA02 ASP 153;ARG 156;HIS 180 mutant C199S
1lldB02 ASP 153;ARG 156;HIS 180 mutant C199S
1lthR02 ASP 153;ARG 156;HIS 180 mutant C199S
1lthT02 ASP 153;ARG 156;HIS 180 mutant C199S
1ceqA02 ASP 168;ARG 171;HIS 195
1cetA02 ASP 168;ARG 171;HIS 195
1ldgA02 ASP 168;ARG 171;HIS 195
1t24A02 ASP 168;ARG 171;HIS 195
1t25A02 ASP 168;ARG 171;HIS 195
1t26A02 ASP 168;ARG 171;HIS 195
1t2cA02 ASP 168;ARG 171;HIS 195
1t2dA02 ASP 154;ARG 157;HIS 181
1t2eA02 ASP 168;ARG 171;HIS 195
1u4oA02 ASP 168;ARG 171;HIS 195
1u4sA02 ASP 168;ARG 171;HIS 195
1u5aA02 ASP 168;ARG 171;HIS 195
1u5cA02 ASP 168;ARG 171;HIS 195
1xivA02 ASP 168;ARG 171;HIS 195
2a94A02 ASP 168;ARG 171;HIS 195
1ldmA02 ASP 166;ARG 169;HIS 193
3ldhA02 ASP 168;ARG 171;HIS 195
6ldhA02 ASP 166;ARG 169;HIS 193
8ldhA02 ASP 166;ARG 169;HIS 193
9ldbA02 ASP 168;ARG 171;HIS 195
9ldbB02 ASP 168;ARG 171;HIS 195
9ldtA02 ASP 168;ARG 171;HIS 195
9ldtB02 ASP 168;ARG 171;HIS 195
5ldhA02 ASP 168;ARG 171;HIS 195
2ldxA02 ASP 165;ARG 168;HIS 192
1i10A02 ASP 165;ARG 168;HIS 192
1i10B02 ASP 165;ARG 168;HIS 192
1i10C02 ASP 165;ARG 168;HIS 192
1i10D02 ASP 165;ARG 168;HIS 192
1i10E02 ASP 165;ARG 168;HIS 192
1i10F02 ASP 165;ARG 168;HIS 192
1i10G02 ASP 165;ARG 168;HIS 192
1i10H02 ASP 165;ARG 168;HIS 192
1i0zA02 ASP 166;ARG 169;HIS 193
1i0zB02 ASP 166;ARG 169;HIS 193
1t2fA02 ASP 166;ARG 169;HIS 193
1t2fB02 ASP 166;ARG 169;HIS 193
1t2fC02 ASP 166;ARG 169;HIS 193
1t2fD02 ASP 166;ARG 169;HIS 193

References for Catalytic Mechanism
References Sections No. 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]
Resource
Comments ATOMIC COORDINATES
Medline ID
PubMed ID 4795361
Journal Biochem Biophys Res Commun
Year 1973
Volume 53
Pages 46-51
Authors Adams MJ, Ford GC, Liljas A, Rossmann MG
Title Atomic co-ordinates for dogfish M4 apo-lactate dehydrogenase.
Related PDB
Related UniProtKB P00341
[2]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 940154
Journal J Mol Biol
Year 1976
Volume 102
Pages 759-79
Authors White JL, Hackert ML, Buehner M, Adams MJ, Ford GC, Lentz PJ Jr, Smiley IE, Steindel SJ, Rossmann MG
Title A comparison of the structures of apo dogfish M4 lactate dehydrogenase and its ternary complexes.
Related PDB 3ldh
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID
PubMed ID 197516
Journal Proc Natl Acad Sci U S A
Year 1977
Volume 74
Pages 2677-81
Authors Eventoff W, Rossmann MG, Taylor SS, Torff HJ, Meyer H, Keil W, Kiltz HH
Title Structural adaptations of lactate dehydrogenase isozymes.
Related PDB
Related UniProtKB P00341
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS)
Medline ID
PubMed ID 468772
Journal J Biol Chem
Year 1979
Volume 254
Pages 7611-20
Authors Musick WD, Rossmann MG
Title The structure of mouse testicular lactate dehydrogenase isoenzyme C4 at 2.9 A resolution.
Related PDB
Related UniProtKB P00342
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
Medline ID
PubMed ID 7338899
Journal J Mol Biol
Year 1981
Volume 151
Pages 289-307
Authors Grau UM, Trommer WE, Rossmann MG
Title Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 A resolution.
Related PDB 5ldh
Related UniProtKB P00336
[6]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 6411465
Journal Eur J Biochem
Year 1983
Volume 134
Pages 503-11
Authors Hensel R, Mayr U, Yang CY
Title The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei.
Related PDB 1llc
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID
PubMed ID
Journal Acta Crystallogr A
Year 1984
Volume 40
Pages 32-4
Authors Buehner M, Hecht HJ
Title Structure determination of the allosteric L-lactate dehydrogenase from Lactobacillus-casei at 3A resolution.
Related PDB
Related UniProtKB P00343
[8]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2443489
Journal J Biol Chem
Year 1987
Volume 262
Pages 13155-62
Authors Hogrefe HH, Griffith JP, Rossmann MG, Goldberg E
Title Characterization of the antigenic sites on the refined 3-A resolution structure of mouse testicular lactate dehydrogenase C4.
Related PDB 2ldx
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (0.25 ANGSTROMS).
Medline ID
PubMed ID 3430615
Journal J Mol Biol
Year 1987
Volume 198
Pages 445-67
Authors Abad-Zapatero C, Griffith JP, Sussman JL, Rossmann MG
Title Refined crystal structure of dogfish M4 apo-lactate dehydrogenase.
Related PDB 1ldm 6ldh 8ldh
Related UniProtKB P00341
[10]
Resource
Comments
Medline ID
PubMed ID 2610514
Journal Appl Biochem Biotechnol
Year 1989
Volume 22
Pages 169-79
Authors Simon ES, Plante R, Whitesides GM
Title D-lactate dehydrogenase. Substrate specificity and use as a catalyst in the synthesis of homochiral 2-hydroxy acids.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 2330370
Journal Proteins
Year 1990
Volume 7
Pages 74-92
Authors Piontek K, Chakrabarti P, Schar HP, Rossmann MG, Zuber H
Title Structure determination and refinement of Bacillus stearothermophilus lactate dehydrogenase.
Related PDB 1ldb 2ldb
Related UniProtKB
[12]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID
PubMed ID 1678537
Journal Philos Trans R Soc Lond B Biol Sci
Year 1991
Volume 332
Pages 177-84
Authors Dunn CR, Wilks HM, Halsall DJ, Atkinson T, Clarke AR, Muirhead H, Holbrook JJ
Title Design and synthesis of new enzymes based on the lactate dehydrogenase framework.
Related PDB 9ldb 9ldt
Related UniProtKB P00339
[13]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID
PubMed ID 1731077
Journal J Mol Biol
Year 1992
Volume 223
Pages 317-35
Authors Wigley DB, Gamblin SJ, Turkenburg JP, Dodson EJ, Piontek K, Muirhead H, Holbrook JJ
Title Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution.
Related PDB 1ldn
Related UniProtKB P00344
[14]
Resource
Comments
Medline ID
PubMed ID 1304374
Journal Protein Sci
Year 1992
Volume 1
Pages 892-901
Authors Cortes A, Emery DC, Halsall DJ, Jackson RM, Clarke AR, Holbrook JJ
Title Charge balance in the alpha-hydroxyacid dehydrogenase vacuole: an acid test.
Related PDB
Related UniProtKB
[15]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID
PubMed ID 8450537
Journal J Mol Biol
Year 1993
Volume 230
Pages 21-7
Authors Iwata S, Ohta T
Title Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase.
Related PDB 1lld
Related UniProtKB P19869
[16]
Resource
Comments
Medline ID
PubMed ID 8120891
Journal J Mol Biol
Year 1994
Volume 1123-4
Pages 236(4)
Authors Goldberg JD, Yoshida T, Brick P
Title Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 A resolution.
Related PDB
Related UniProtKB
[17]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID
PubMed ID 7656036
Journal Nat Struct Biol
Year 1994
Volume 1
Pages 176-85
Authors Iwata S, Kamata K, Yoshida S, Minowa T, Ohta T
Title T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control.
Related PDB 1lth
Related UniProtKB P19869
[18]
Resource
Comments
Medline ID
PubMed ID 8532681
Journal Protein Eng
Year 1995
Volume 8
Pages 565-73
Authors Philippopoulos M, Xiang Y, Lim C
Title Identifying the mechanism of protein loop closure: a molecular dynamics simulation of the Bacillus stearothermophilus LDH loop in solution.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS)
Medline ID
PubMed ID 8901865
Journal Nat Struct Biol
Year 1996
Volume 3
Pages 912-5
Authors Dunn CR, Banfield MJ, Barker JJ, Higham CW, Moreton KM, Turgut-Balik D, Brady RL, Holbrook JJ
Title The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design.
Related PDB 1ceq 1ldg
Related UniProtKB Q27743
[20]
Resource
Comments
Medline ID
PubMed ID 9162946
Journal Proteins
Year 1996
Volume 24
Pages 450-66
Authors van der Spoel D, Vogel HJ, Berendsen HJ
Title Molecular dynamics simulations of N-terminal peptides from a nucleotide binding protein.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 9017191
Journal Biophys J
Year 1997
Volume 72
Pages 619-26
Authors van Beek J, Callender R, Gunner MR
Title The contribution of electrostatic and van der Waals interactions to the stereospecificity of the reaction catalyzed by lactate dehydrogenase.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 9329087
Journal Proteins
Year 1997
Volume 29
Pages 228-39
Authors Dafforn TR, Badcoe IG, Sessions RB, el Hawrani AS, Holbrook JJ
Title Correlation of the enzyme activities of Bacillus stearothermophilus lactate dehydrogenase on three substrates with the results of molecular dynamics/energy minimization conformational searching.
Related PDB
Related UniProtKB
[23]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
Medline ID
PubMed ID 9655830
Journal Structure
Year 1998
Volume 6
Pages 769-81
Authors Auerbach G, Ostendorp R, Prade L, Korndorfer I, Dams T, Huber R, Jaenicke R
Title Lactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization.
Related PDB 1a5z
Related UniProtKB P16115
[24]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10187806
Journal J Biol Chem
Year 1999
Volume 274
Pages 10213-8
Authors Read JA, Wilkinson KW, Tranter R, Sessions RB, Brady RL
Title Chloroquine binds in the cofactor binding site of Plasmodium falciparum lactate dehydrogenase.
Related PDB 1cet
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 10556245
Journal Protein Eng
Year 1999
Volume 12
Pages 851-6
Authors Holmberg N, Ryde U, Bulow L
Title Redesign of the coenzyme specificity in L-lactate dehydrogenase from bacillus stearothermophilus using site-directed mutagenesis and media engineering.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 10951199
Journal Eur J Biochem
Year 2000
Volume 267
Pages 5413-20
Authors Berr K, Wassenberg D, Lilie H, Behlke J, Jaenicke R
Title epsilon-crystallin from duck eye lens comparison of its quaternary structure and stability with other lactate dehydrogenases and complex formation with alpha-crystallin.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 11401572
Journal Biochemistry
Year 2001
Volume 40
Pages 7247-52
Authors Kedzierski P, Moreton K, Clarke AR, Holbrook JJ
Title The A245K mutation exposes another stage of the bacterial L-lactate dehydrogenase reaction mechanism.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 11292347
Journal J Mol Biol
Year 2001
Volume 307
Pages 1351-62
Authors Lee BI, Chang C, Cho SJ, Eom SH, Kim KK, Yu YG, Suh SW
Title Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases.
Related PDB
Related UniProtKB
[29]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11276087
Journal Proteins
Year 2001
Volume 43
Pages 175-85
Authors Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL
Title Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase.
Related PDB 1i0z 1i10
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 11807949
Journal Proteins
Year 2002
Volume 46
Pages 206-14
Authors Uchikoba H, Fushinobu S, Wakagi T, Konno M, Taguchi H, Matsuzawa H
Title Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfaces.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 12967707
Journal Mol Biochem Parasitol
Year 2003
Volume 131
Pages 1-10
Authors Winter VJ, Cameron A, Tranter R, Sessions RB, Brady RL
Title Crystal structure of Plasmodium berghei lactate dehydrogenase indicates the unique structural differences of these enzymes are shared across the Plasmodium genus.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 15147206
Journal Biochemistry
Year 2004
Volume 43
Pages 6219-29
Authors Brown WM, Yowell CA, Hoard A, Vander Jagt TA, Hunsaker LA, Deck LM, Royer RE, Piper RC, Dame JB, Makler MT, Vander Jagt DL
Title Comparative structural analysis and kinetic properties of lactate dehydrogenases from the four species of human malarial parasites.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 15117937
Journal J Biol Chem
Year 2004
Volume 279
Pages 31429-39
Authors Cameron 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
Title Identification and activity of a series of azole-based compounds with lactate dehydrogenase-directed anti-malarial activity.
Related PDB 1t2f 1t24 1t25 1t26 1t2c 1t2d 1t2e
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 15978953
Journal Mol Biochem Parasitol
Year 2005
Volume 142
Pages 137-48
Authors Conners R, Schambach F, Read J, Cameron A, Sessions RB, Vivas L, Easton A, Croft SL, Brady RL
Title Mapping the binding site for gossypol-like inhibitors of Plasmodium falciparum lactate dehydrogenase.
Related PDB 1u4o 1u4s 1u5a 1u5c 1xiv
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 16331982
Journal Biochemistry
Year 2005
Volume 44
Pages 16221-8
Authors Chaikuad A, Fairweather V, Conners R, Joseph-Horne T, Turgut-Balik D, Brady RL
Title Structure of lactate dehydrogenase from Plasmodium vivax: complexes with NADH and APADH.
Related PDB 2a94
Related UniProtKB

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

Created Updated
2004-12-01 2012-06-25