D00456
type: Enzyme
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.1.1.28
csa: 1j49
uniprot: P30901
uniprot: P26297
kegg enzyme: D-lactate dehydrogenase
kegg enzyme: lactic acid dehydrogenase
kegg enzyme: D-specific lactic dehydrogenase
kegg enzyme: D-(-)-lactate dehydrogenase (NAD+)
kegg enzyme: D-lactic acid dehydrogenase
kegg enzyme: D-lactic dehydrogenase
kegg pathway: Pyruvate metabolism
kegg substrate: (R)-Lactate
kegg substrate: NAD+
kegg product: Pyruvate
kegg product: NADH
kegg product: H+
pdb: 2dldA01
pdb: 2dldB01
pdb: 1j49A01
pdb: 1j49B01
pdb: 1j4aA01
pdb: 1j4aB01
pdb: 1j4aC01
pdb: 1j4aD01
pdb: 2dldA02
pdb: 2dldB02
pdb: 1j49A02
pdb: 1j49B02
pdb: 1j4aA02
pdb: 1j4aB02
pdb: 1j4aC02
pdb: 1j4aD02
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 2dldA01
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 2dldB01
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j49A01
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j49B01
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j4aA01
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j4aB01
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j4aC01
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j4aD01
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 2dldA02
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 2dldB02
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j49A02
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j49B02
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j4aA02
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j4aB02
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j4aC02
pdb bound state: Unbound
  compound: (R)-Lactate
  pdb: 1j4aD02
pdb bound state: Unbound
  compound: NAD+
  pdb: 2dldA01
pdb bound state: Unbound
  compound: NAD+
  pdb: 2dldB01
active site residues resources: Involvement of Glu-264 and Arg-235 in the essential interaction between the catalytic imidazole and substrate for the D-lactate dehydrogenase catalysis.
active site residues resources: Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution.
active site residues resources: Novel substrate specificity of designer 3-isopropylmalate dehydrogenase derived from Thermus thermophilus HB8.
active site residues resources: P30901
references: Salt-induced alteration of D(-) lactate dehydrogenase from Polyspondylium pallidum.
references: Diphosphopyridine nucleotide-linked D-lactate dehydrogenases from the horseshoe crab, Limulus polyphemus, and the seaworm, Nereis virens. II. Catalytic properties.
references: Steady-state kinetic studies on D-lactate dehydrogenase from Megasphera elsdenii.
references: Comparison of the D-lactate stereospecific dehydrogenase of Limulus polyphemus with active-site regions of L-lactate dehydrogenases.
references: Multiple molecular forms of Acanthamoeba lactic dehydrogenase.
references: D-lactate dehydrogenase. Substrate specificity and use as a catalyst in the synthesis of homochiral 2-hydroxy acids.
references: Nonpolar interactions in the maleimide inactivation of Haemophilus influenzae D-lactate dehydrogenase.
references: Lactate dehydrogenase from the extreme halophilic archaebacterium Halobacterium marismortui.
references: Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases.
references: Prediction of structurally conserved regions of D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase.
references: Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase.
references: Essential role of arginine 235 in the substrate-binding of Lactobacillus plantarum D-lactate dehydrogenase.
references: Crystallization of D-lactate dehydrogenase from Lactobacillus bulgaricus.
references: Knowledge-based modeling of the D-lactate dehydrogenase three-dimensional structure.
references: 13C nuclear magnetic resonance analysis of glucose and citrate end products in an ldhL-ldhD double-knockout strain of Lactobacillus plantarum.
references: Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase.
references: Involvement of Glu-264 and Arg-235 in the essential interaction between the catalytic imidazole and substrate for the D-lactate dehydrogenase catalysis.
references: Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution.
references: A thioredoxin fusion protein of VanH, a D-lactate dehydrogenase from Enterococcus faecium: cloning, expression, purification, kinetic analysis, and crystallization.
references: Roles of his205, his296, his303 and Asp259 in catalysis by NAD+-specific D-lactate dehydrogenase.
references: Novel substrate specificity of designer 3-isopropylmalate dehydrogenase derived from Thermus thermophilus HB8.
references: Identification of putative mammalian D-lactate dehydrogenase enzymes.
references: Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.
comment: This enzyme may have a similar catalytic mechanism to that of glycerate dehydrogenase (D00457 in EzCatDB), as they share a similar active-site.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720
catalytic domain: index.html

Pyruvate metabolism
type: KeggPathway
references: KEGG:MAP00620

(R)-Lactate
type: KeggSubstrate
references: KEGG:C00256
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:42111
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NAD+
type: KeggSubstrate
references: KEGG:C00003
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pyruvate
type: KeggProduct
references: KEGG:C00022
compound type: carbohydrate
compound type: carboxyl group
references: CHEBI:32816
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADH
type: KeggProduct
references: KEGG:C00004
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H+
type: KeggProduct
references: KEGG:C00080
compound type: others
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

2dldA02
type: Pdb
references: 2dld
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2dld
catalytic residue: HIS 206;ARG 236;ASP 260;GLU 265;HIS 297

2dldB02
type: Pdb
references: 2dld
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2dld
catalytic residue: HIS 206;ARG 236;ASP 260;GLU 265;HIS 297

1j49A02
type: Pdb
references: 1j49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j49
catalytic residue: HIS 206;ARG 236;ASP 260;GLU 265;HIS 297

1j49B02
type: Pdb
references: 1j49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j49
catalytic residue: HIS 206;ARG 236;ASP 260;GLU 265;HIS 297

1j4aA02
type: Pdb
references: 1j4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j4a
catalytic residue: HIS 206;ARG 236;ASP 260;GLU 265;
comment: mutant H297K

1j4aB02
type: Pdb
references: 1j4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j4a
catalytic residue: HIS 206;ARG 236;ASP 260;GLU 265;
comment: mutant H297K

1j4aC02
type: Pdb
references: 1j4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j4a
catalytic residue: HIS 206;ARG 236;ASP 260;GLU 265;
comment: mutant H297K

1j4aD02
type: Pdb
references: 1j4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1j4a
catalytic residue: HIS 206;ARG 236;ASP 260;GLU 265;
comment: mutant H297K

Salt-induced alteration of D(-) lactate dehydrogenase from Polyspondylium pallidum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4291632
journal: Biochem Biophys Res Commun
volume: 26
pages: 679-85
published year: 1967
authors:
  item: Garland RC
  item: Kaplan NO

Diphosphopyridine nucleotide-linked D-lactate dehydrogenases from the horseshoe crab, Limulus polyphemus, and the seaworm, Nereis virens. II. Catalytic properties.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/4348014
journal: Arch Biochem Biophys
volume: 154
pages: 711-25
published year: 1973
authors:
  item: Long GL
  item: Kaplan NO

Steady-state kinetic studies on D-lactate dehydrogenase from Megasphera elsdenii.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7074087
journal: Biochemistry
volume: 21
pages: 1307-12
published year: 1982
authors:
  item: Morpeth FF
  item: Massey V

Comparison of the D-lactate stereospecific dehydrogenase of Limulus polyphemus with active-site regions of L-lactate dehydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6652095
journal: Biochim Biophys Acta
volume: 749
pages: 153-62
published year: 1983
authors:
  item: Siebenaller JF
  item: Orr TL
  item: Olwin BB
  item: Taylor SS

Multiple molecular forms of Acanthamoeba lactic dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3248371
journal: Comp Biochem Physiol B
volume: 90
pages: 833-6
published year: 1988
authors:
  item: Ward AP
  item: al-Abidin NZ

D-lactate dehydrogenase. Substrate specificity and use as a catalyst in the synthesis of homochiral 2-hydroxy acids.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2610514
journal: Appl Biochem Biotechnol
volume: 22
pages: 169-79
published year: 1989
authors:
  item: Simon ES
  item: Plante R
  item: Whitesides GM

Nonpolar interactions in the maleimide inactivation of Haemophilus influenzae D-lactate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2378905
journal: Biochim Biophys Acta
volume: 1040
pages: 84-8
published year: 1990
authors:
  item: Denicola-Seoane A
  item: Anderson BM

Lactate dehydrogenase from the extreme halophilic archaebacterium Halobacterium marismortui.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2117936
journal: Biol Chem Hoppe Seyler
volume: 371
pages: 515-9
published year: 1990
authors:
  item: Hecht K
  item: Langer T
  item: Wrba A
  item: Jaenicke R

Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1567457
journal: Biochem Biophys Res Commun
volume: 184
pages: 60-6
published year: 1992
authors:
  item: Kochhar S
  item: Hunziker PE
  item: Leong-Morgenthaler P
  item: Hottinger H

Prediction of structurally conserved regions of D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8476420
journal: Biochem Biophys Res Commun
volume: 192
pages: 182-8
published year: 1993
authors:
  item: Vinals C
  item: Depiereux E
  item: Feytmans E

Histidine 296 is essential for the catalysis in Lactobacillus plantarum D-lactate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8349682
journal: J Biol Chem
volume: 268
pages: 18030-4
published year: 1993
authors:
  item: Taguchi H
  item: Ohta T

Essential role of arginine 235 in the substrate-binding of Lactobacillus plantarum D-lactate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7961609
journal: J Biochem (Tokyo)
volume: 115
pages: 930-6
published year: 1994
authors:
  item: Taguchi H
  item: Ohta T

Crystallization of D-lactate dehydrogenase from Lactobacillus bulgaricus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8289259
journal: J Mol Biol
volume: 235
pages: 370-1
published year: 1994
authors:
  item: Nessler S
  item: Le Bras G
  item: Garel JR

Knowledge-based modeling of the D-lactate dehydrogenase three-dimensional structure.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7567953
journal: Proteins
volume: 21
pages: 307-18
published year: 1995
authors:
  item: Vinals C
  item: De Bolle X
  item: Depiereux E
  item: Feytmans E
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

13C nuclear magnetic resonance analysis of glucose and citrate end products in an ldhL-ldhD double-knockout strain of Lactobacillus plantarum.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8955418
journal: J Bacteriol
volume: 178
pages: 7311-5
published year: 1996
authors:
  item: Ferain T
  item: Schanck AN
  item: Delcour J

Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8740366
journal: Structure
volume: 4
pages: 437-47
published year: 1996
authors:
  item: Stoll VS
  item: Kimber MS
  item: Pai EF

Involvement of Glu-264 and Arg-235 in the essential interaction between the catalytic imidazole and substrate for the D-lactate dehydrogenase catalysis.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9399585
journal: J Biochem (Tokyo)
volume: 122
pages: 802-9
published year: 1997
authors:
  item: Taguchi H
  item: Ohta T
  item: Matsuzawa H

Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9126843
journal: J Mol Biol
volume: 267
pages: 640-60
published year: 1997
authors:
  item: Dengler U
  item: Niefind K
  item: Kiess M
  item: Schomburg D

A thioredoxin fusion protein of VanH, a D-lactate dehydrogenase from Enterococcus faecium: cloning, expression, purification, kinetic analysis, and crystallization.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9605319
journal: Protein Sci
volume: 7
pages: 1147-55
published year: 1998
authors:
  item: Stoll VS
  item: Manohar AV
  item: Gillon W
  item: MacFarlane EL
  item: Hynes RC
  item: Pai EF

Roles of his205, his296, his303 and Asp259 in catalysis by NAD+-specific D-lactate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10712593
journal: Eur J Biochem
volume: 267
pages: 1633-9
published year: 2000
authors:
  item: Kochhar S
  item: Lamzin VS
  item: Razeto A
  item: Delley M
  item: Hottinger H
  item: Germond JE

Novel substrate specificity of designer 3-isopropylmalate dehydrogenase derived from Thermus thermophilus HB8.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11826966
journal: Biosci Biotechnol Biochem
volume: 65
pages: 2695-700
published year: 2001
authors:
  item: Fujita M
  item: Tamegai H
  item: Eguchi T
  item: Kakinuma K

Identification of putative mammalian D-lactate dehydrogenase enzymes.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12127981
journal: Biochem Biophys Res Commun
volume: 295
pages: 910-6
published year: 2002
authors:
  item: Flick MJ
  item: Konieczny SF

Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12054772
journal: J Mol Biol
volume: 318
pages: 109-19
published year: 2002
authors:
  item: Razeto A
  item: Kochhar S
  item: Hottinger H
  item: Dauter M
  item: Wilson KS
  item: Lamzin VS
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Analogue
compound: Pyruvate
pdb: 2dldA02
ligand het code: OXM

Analogue
compound: Pyruvate
pdb: 2dldB02
ligand het code: OXM

ReferenceForCatalyticMechanism
reference index: 11

ReferenceForCatalyticMechanism
reference index: 12
reference section: Fig.6, p.936

ReferenceForCatalyticMechanism
reference index: 16

ReferenceForCatalyticMechanism
reference index: 17
reference section: Fig.6

ReferenceForCatalyticMechanism
reference index: 18
reference section: p.653-655

ReferenceForCatalyticMechanism
reference index: 20

ReferenceForCatalyticMechanism
reference index: 23
reference section: p.113