EzCatDB: M00001
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DB codeM00001
CATH domainDomain 13.30.70.610 : Alpha-Beta Plaits
Domain 23.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Domain 33.30.465.20 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3Catalytic domain
Domain 43.30.1370.20 : Ribosomal Protein S8; Chain
E.C.1.1.1.28

CATH domainRelated DB codes (homologues)
3.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2M00004,M00039,M00179,T00003
3.30.465.20 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3M00004,M00179

Enzyme Name
UniProtKBKEGG

P06149
Protein nameD-lactate dehydrogenaseD-lactate dehydrogenase
lactic acid dehydrogenase
lactic acid dehydrogenase
D-specific lactic dehydrogenase
D-(-)-lactate dehydrogenase (NAD+)
D-lactic acid dehydrogenase
D-lactic dehydrogenase
SynonymsEC 1.1.1.28
Respiratory D-lactate dehydrogenase
RefSeqNP_416637.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_490372.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF01565 (FAD_binding_4)
PF09330 (Lact-deh-memb)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00620Pyruvate metabolism

UniProtKB:Accession NumberP06149
Entry nameDLD_ECOLI
Activity(R)-lactate + NAD(+) = pyruvate + NADH.
Subunit
Subcellular locationCell membrane, Peripheral membrane protein, Cytoplasmic side.
CofactorFAD.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00016C00256C00003C00022C00004
CompoundFAD(R)-LactateNAD+PyruvateNADH
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotidecarbohydrate,carboxyl groupamide group,amine group,nucleotidecarbohydrate,carboxyl groupamide group,amine group,nucleotide
ChEBI16238
42111
15846
32816
16908
PubChem643975
61503
5893
1060
439153
             
1f0xA01UnboundUnboundUnboundUnboundUnbound
1f0xB01UnboundUnboundUnboundUnboundUnbound
1f0xA02UnboundUnboundUnboundUnboundUnbound
1f0xB02UnboundUnboundUnboundUnboundUnbound
1f0xA03Bound:FADUnboundUnboundUnboundUnbound
1f0xB03Bound:FADUnboundUnboundUnboundUnbound
1f0xA04UnboundUnboundUnboundUnboundUnbound
1f0xB04UnboundUnboundUnboundUnboundUnbound

Active-site residues
pdb
        
1f0xA01
1f0xB01
1f0xA02
1f0xB02
1f0xA03
1f0xB03
1f0xA04
1f0xB04

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[9]p.9415

references
[1]
PubMed ID4565667
JournalJ Biol Chem
Year1972
Volume247
Pages7858-63
AuthorsWalsh CT, Abeles RH, Kaback HR
TitleMechanisms of active transport in isolated bacterial membrane vesicles. X. Inactivation of D-lactate dehydrogenase and D-lactate dehydrogenase-coupled transport in Escherichia coli membrane vesicles by an acetylenic substrate.
[2]
PubMed ID4582730
JournalJ Biol Chem
Year1973
Volume248
Pages7012-7
AuthorsKohn LD, Kaback HR
TitleMechanisms of active transport in isolated bacterial membrane vesicles. XV. Purification and properties of the membrane-bound D-lactate dehydrogenase from.
[3]
PubMed ID7026558
JournalJ Biol Chem
Year1981
Volume256
Pages10369-74
AuthorsKovatchev S, Vaz WL, Eibl H
TitleLipid dependence of the membrane-bound D-lactate dehydrogenase of Escherichia coli.
[4]
PubMed ID3548821
JournalBiochemistry
Year1987
Volume26
Pages549-56
AuthorsRule GS, Pratt EA, Simplaceanu V, Ho C
TitleNuclear magnetic resonance and molecular genetic studies of the membrane-bound D-lactate dehydrogenase of Escherichia coli.
[5]
PubMed ID2185834
JournalBiochemistry
Year1990
Volume29
Pages3256-62
AuthorsPeersen OB, Pratt EA, Truong HT, Ho C, Rule GS
TitleSite-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: a 19F nuclear magnetic resonance study.
[6]
PubMed ID1850292
JournalBiochemistry
Year1991
Volume30
Pages3893-8
AuthorsTruong HT, Pratt EA, Ho C
TitleInteraction of the membrane-bound D-lactate dehydrogenase of Escherichia coli with phospholipid vesicles and reconstitution of activity using a spin-labeled fatty acid as an electron acceptor: a magnetic resonance and biochemical study.
[7]
PubMed ID1931992
JournalBiochemistry
Year1991
Volume30
Pages10722-9
AuthorsTruong HT, Pratt EA, Rule GS, Hsue PY, Ho C
TitleInactive and temperature-sensitive folding mutants generated by tryptophan substitutions in the membrane-bound d-lactate dehydrogenase of Escherichia coli.
[8]
PubMed ID8987983
JournalBiochemistry
Year1996
Volume35
Pages16502-9
AuthorsSun ZY, Pratt EA, Simplaceanu V, Ho C
TitleA 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID20402548
PubMed ID10944213
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages9413-8
AuthorsDym O, Pratt EA, Ho C, Eisenberg D
TitleThe crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme.
Related PDB1f0x
Related UniProtKBP06149


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2004-03-252009-02-26


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