DB code: D00456
CATH domain | 3.40.50.720 : Rossmann fold | |
---|---|---|
3.40.50.720 : Rossmann fold | Catalytic domain | |
E.C. | 1.1.1.28 | |
CSA | 1j49 | |
M-CSA | 1j49 | |
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 D00457 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 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 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam | RefSeq |
---|---|---|---|---|
P30901 |
D-lactate dehydrogenase
|
D-LDH
EC 1.1.1.28 D-specific D-2-hydroxyacid dehydrogenase |
PF00389
(2-Hacid_dh)
PF02826 (2-Hacid_dh_C) [Graphical View] |
|
P26297 |
D-lactate dehydrogenase
|
D-LDH
EC 1.1.1.28 D-specific D-2-hydroxyacid dehydrogenase |
PF00389
(2-Hacid_dh)
PF02826 (2-Hacid_dh_C) [Graphical View] |
YP_618304.1
(Protein)
NC_008054.1 (DNA/RNA sequence) |
KEGG enzyme name |
---|
D-lactate dehydrogenase
lactic acid dehydrogenase lactic acid dehydrogenase D-specific lactic dehydrogenase D-(-)-lactate dehydrogenase (NAD+) D-lactic acid dehydrogenase D-lactic dehydrogenase |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P30901 | LDHD_LACHE | (R)-lactate + NAD(+) = pyruvate + NADH. | Homodimer. | ||
P26297 | LDHD_LACDA | (R)-lactate + NAD(+) = pyruvate + NADH. | Homodimer. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00620 | Pyruvate metabolism |
Compound table | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | |||||||||
KEGG-id | C00256 | C00003 | C00022 | C00004 | C00080 | ||||||
E.C. | |||||||||||
Compound | (R)-Lactate | NAD+ | Pyruvate | NADH | H+ | ||||||
Type | carbohydrate,carboxyl group | amide group,amine group,nucleotide | carbohydrate,carboxyl group | amide group,amine group,nucleotide | others | ||||||
ChEBI |
42111 42111 |
15846 15846 |
32816 32816 |
16908 16908 |
15378 15378 |
||||||
PubChem |
61503 61503 |
5893 5893 |
1060 1060 |
439153 439153 |
1038 1038 |
||||||
2dldA01 | Unbound | Unbound | Unbound | Unbound | |||||||
2dldB01 | Unbound | Unbound | Unbound | Unbound | |||||||
1j49A01 | Unbound | Unbound | Unbound | Unbound | |||||||
1j49B01 | Unbound | Unbound | Unbound | Unbound | |||||||
1j4aA01 | Unbound | Unbound | Unbound | Unbound | |||||||
1j4aB01 | Unbound | Unbound | Unbound | Unbound | |||||||
1j4aC01 | Unbound | Unbound | Unbound | Unbound | |||||||
1j4aD01 | Unbound | Unbound | Unbound | Unbound | |||||||
2dldA02 | Unbound | Bound:NAD | Analogue:OXM | Unbound | |||||||
2dldB02 | Unbound | Bound:NAD | Analogue:OXM | Unbound | |||||||
1j49A02 | Unbound | Bound:NAD | Unbound | Unbound | |||||||
1j49B02 | Unbound | Bound:NAD | Unbound | Unbound | |||||||
1j4aA02 | Unbound | Unbound | Unbound | Unbound | |||||||
1j4aB02 | Unbound | Unbound | Unbound | Unbound | |||||||
1j4aC02 | Unbound | Unbound | Unbound | Unbound | |||||||
1j4aD02 | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Swiss-prot;P30901 & literature [16], [17] & [20] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
2dldA01 | ||||||||||
2dldB01 | ||||||||||
1j49A01 | ||||||||||
1j49B01 | ||||||||||
1j4aA01 | ||||||||||
1j4aB01 | ||||||||||
1j4aC01 | ||||||||||
1j4aD01 | ||||||||||
2dldA02 | HIS 206;ARG 236;ASP 260;GLU 265;HIS 297 | |||||||||
2dldB02 | HIS 206;ARG 236;ASP 260;GLU 265;HIS 297 | |||||||||
1j49A02 | HIS 206;ARG 236;ASP 260;GLU 265;HIS 297 | |||||||||
1j49B02 | HIS 206;ARG 236;ASP 260;GLU 265;HIS 297 | |||||||||
1j4aA02 | HIS 206;ARG 236;ASP 260;GLU 265; | mutant H297K | ||||||||
1j4aB02 | HIS 206;ARG 236;ASP 260;GLU 265; | mutant H297K | ||||||||
1j4aC02 | HIS 206;ARG 236;ASP 260;GLU 265; | mutant H297K | ||||||||
1j4aD02 | HIS 206;ARG 236;ASP 260;GLU 265; | mutant H297K |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[11]
|
||
[12]
|
Fig.6, p.936 | |
[16]
|
||
[17]
|
Fig.6 | |
[18]
|
p.653-655 | |
[20]
|
||
[23]
|
p.113 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 4291632 |
Journal | Biochem Biophys Res Commun |
Year | 1967 |
Volume | 26 |
Pages | 679-85 |
Authors | Garland RC, Kaplan NO |
Title | Salt-induced alteration of D(-) lactate dehydrogenase from Polyspondylium pallidum. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 4348014 |
Journal | Arch Biochem Biophys |
Year | 1973 |
Volume | 154 |
Pages | 711-25 |
Authors | Long GL, Kaplan NO |
Title |
Diphosphopyridine nucleotide-linked D-lactate dehydrogenases from the horseshoe crab, |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7074087 |
Journal | Biochemistry |
Year | 1982 |
Volume | 21 |
Pages | 1307-12 |
Authors | Morpeth FF, Massey V |
Title | Steady-state kinetic studies on D-lactate dehydrogenase from Megasphera elsdenii. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 6652095 |
Journal | Biochim Biophys Acta |
Year | 1983 |
Volume | 749 |
Pages | 153-62 |
Authors | Siebenaller JF, Orr TL, Olwin BB, Taylor SS |
Title | Comparison of the D-lactate stereospecific dehydrogenase of Limulus polyphemus with active-site regions of L-lactate dehydrogenases. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 3248371 |
Journal | Comp Biochem Physiol B |
Year | 1988 |
Volume | 90 |
Pages | 833-6 |
Authors | Ward AP, al-Abidin NZ |
Title | Multiple molecular forms of Acanthamoeba lactic dehydrogenase. |
Related PDB | |
Related UniProtKB | |
[6] | |
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. |
Related PDB | |
Related UniProtKB | |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2378905 |
Journal | Biochim Biophys Acta |
Year | 1990 |
Volume | 1040 |
Pages | 84-8 |
Authors | Denicola-Seoane A, Anderson BM |
Title | Nonpolar interactions in the maleimide inactivation of Haemophilus influenzae D-lactate dehydrogenase. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2117936 |
Journal | Biol Chem Hoppe Seyler |
Year | 1990 |
Volume | 371 |
Pages | 515-9 |
Authors | Hecht K, Langer T, Wrba A, Jaenicke R |
Title | Lactate dehydrogenase from the extreme halophilic archaebacterium Halobacterium marismortui. |
Related PDB | |
Related UniProtKB | |
[9] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1567457 |
Journal | Biochem Biophys Res Commun |
Year | 1992 |
Volume | 184 |
Pages | 60-6 |
Authors | Kochhar S, Hunziker PE, Leong-Morgenthaler P, Hottinger H |
Title | Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases. |
Related PDB | |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8476420 |
Journal | Biochem Biophys Res Commun |
Year | 1993 |
Volume | 192 |
Pages | 182-8 |
Authors | Vinals C, Depiereux E, Feytmans E |
Title | Prediction of structurally conserved regions of D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase. |
Related PDB | |
Related UniProtKB | |
[11] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8349682 |
Journal | J Biol Chem |
Year | 1993 |
Volume | 268 |
Pages | 18030-4 |
Authors | Taguchi H, Ohta T |
Title | Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase. |
Related PDB | |
Related UniProtKB | |
[12] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7961609 |
Journal | J Biochem (Tokyo) |
Year | 1994 |
Volume | 115 |
Pages | 930-6 |
Authors | Taguchi H, Ohta T |
Title | Essential role of arginine 235 in the substrate-binding of Lactobacillus plantarum D-lactate dehydrogenase. |
Related PDB | |
Related UniProtKB | |
[13] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8289259 |
Journal | J Mol Biol |
Year | 1994 |
Volume | 235 |
Pages | 370-1 |
Authors | Nessler S, Le Bras G, Le Bras G, Garel JR |
Title | Crystallization of D-lactate dehydrogenase from Lactobacillus bulgaricus. |
Related PDB | |
Related UniProtKB | |
[14] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7567953 |
Journal | Proteins |
Year | 1995 |
Volume | 21 |
Pages | 307-18 |
Authors | Vinals C, De Bolle X, Depiereux E, Feytmans E |
Title | Knowledge-based modeling of the D-lactate dehydrogenase three-dimensional structure. |
Related PDB | 1dld |
Related UniProtKB | |
[15] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8955418 |
Journal | J Bacteriol |
Year | 1996 |
Volume | 178 |
Pages | 7311-5 |
Authors | Ferain T, Schanck AN, Delcour J |
Title | 13C nuclear magnetic resonance analysis of glucose and citrate end products in an ldhL-ldhD double-knockout strain of Lactobacillus plantarum. |
Related PDB | |
Related UniProtKB | |
[16] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8740366 |
Journal | Structure |
Year | 1996 |
Volume | 4 |
Pages | 437-47 |
Authors | Stoll VS, Kimber MS, Pai EF |
Title | Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase. |
Related PDB | |
Related UniProtKB | |
[17] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9399585 |
Journal | J Biochem (Tokyo) |
Year | 1997 |
Volume | 122 |
Pages | 802-9 |
Authors | Taguchi H, Ohta T, Matsuzawa H |
Title | Involvement of Glu-264 and Arg-235 in the essential interaction between the catalytic imidazole and substrate for the D-lactate dehydrogenase catalysis. |
Related PDB | |
Related UniProtKB | |
[18] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9126843 |
Journal | J Mol Biol |
Year | 1997 |
Volume | 267 |
Pages | 640-60 |
Authors | Dengler U, Niefind K, Kiess M, Schomburg D |
Title |
Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, |
Related PDB | |
Related UniProtKB | |
[19] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9605319 |
Journal | Protein Sci |
Year | 1998 |
Volume | 7 |
Pages | 1147-55 |
Authors | Stoll VS, Manohar AV, Gillon W, MacFarlane EL, Hynes RC, Pai EF |
Title |
A thioredoxin fusion protein of VanH, |
Related PDB | |
Related UniProtKB | |
[20] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10712593 |
Journal | Eur J Biochem |
Year | 2000 |
Volume | 267 |
Pages | 1633-9 |
Authors | Kochhar S, Lamzin VS, Razeto A, Delley M, Hottinger H, Germond JE |
Title |
Roles of his205, |
Related PDB | |
Related UniProtKB | |
[21] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11826966 |
Journal | Biosci Biotechnol Biochem |
Year | 2001 |
Volume | 65 |
Pages | 2695-700 |
Authors | Fujita M, Tamegai H, Eguchi T, Kakinuma K |
Title | Novel substrate specificity of designer 3-isopropylmalate dehydrogenase derived from Thermus thermophilus HB8. |
Related PDB | |
Related UniProtKB | |
[22] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12127981 |
Journal | Biochem Biophys Res Commun |
Year | 2002 |
Volume | 295 |
Pages | 910-6 |
Authors | Flick MJ, Konieczny SF |
Title | Identification of putative mammalian D-lactate dehydrogenase enzymes. |
Related PDB | |
Related UniProtKB | |
[23] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12054772 |
Journal | J Mol Biol |
Year | 2002 |
Volume | 318 |
Pages | 109-19 |
Authors | Razeto A, Kochhar S, Hottinger H, Dauter M, Wilson KS, Lamzin VS |
Title |
Domain closure, |
Related PDB | 1j49 1j4a |
Related UniProtKB |
Comments |
---|
This enzyme may have a similar catalytic mechanism to that of glycerate dehydrogenase (D00457 in EzCatDB), |
Created | Updated |
---|---|
2004-12-01 | 2009-02-26 |