KEGG   ENZYME: 1.1.1.345Help
Entry
EC 1.1.1.345                Enzyme                                 

Name
D-2-hydroxyacid dehydrogenase (NAD+);
LdhA;
HdhD;
D-2-hydroxyisocaproate dehydrogenase;
R-HicDH;
D-HicDH;
(R)-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase;
(R)-2-hydroxyisocaproate dehydrogenase;
D-mandelate dehydrogenase (ambiguous)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
(R)-2-hydroxycarboxylate:NAD+ oxidoreductase
Reaction(IUBMB)
an (R)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+ [RN:R10222]
Reaction(KEGG)
Substrate
(R)-2-hydroxycarboxylate [CPD:C02489];
NAD+ [CPD:C00003]
Product
2-oxocarboxylate [CPD:C00161];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+).
History
EC 1.1.1.345 created 2013
Reference
1  [PMID:9126843]
  Authors
Dengler U, Niefind K, Kiess M, Schomburg D
  Title
Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution.
  Journal
J Mol Biol 267:640-60 (1997)
DOI:10.1006/jmbi.1996.0864
Reference
2  [PMID:11120357]
  Authors
Bonete MJ, Ferrer J, Pire C, Penades M, Ruiz JL
  Title
2-Hydroxyacid dehydrogenase from Haloferax mediterranei, a D-isomer-specific member of the 2-hydroxyacid dehydrogenase family.
  Journal
Biochimie 82:1143-50 (2000)
DOI:10.1016/S0300-9084(00)01193-7
Reference
3  [PMID:16957230]
  Authors
Kim J, Darley D, Selmer T, Buckel W
  Title
Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile.
  Journal
Appl Environ Microbiol 72:6062-9 (2006)
DOI:10.1128/AEM.00772-06
  Sequence
Reference
4  [PMID:18391442]
  Authors
Wada Y, Iwai S, Tamura Y, Ando T, Shinoda T, Arai K, Taguchi H
  Title
A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases.
  Journal
Biosci Biotechnol Biochem 72:1087-94 (2008)
DOI:10.1271/bbb.70827
Reference
5  [PMID:19047348]
  Authors
Chambellon E, Rijnen L, Lorquet F, Gitton C, van Hylckama Vlieg JE, Wouters JA, Yvon M
  Title
The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis.
  Journal
J Bacteriol 191:873-81 (2009)
DOI:10.1128/JB.01114-08
Reference
6  [PMID:23954635]
  Authors
Miyanaga A, Fujisawa S, Furukawa N, Arai K, Nakajima M, Taguchi H
  Title
The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase.
  Journal
Biochem Biophys Res Commun 439:109-14 (2013)
DOI:10.1016/j.bbrc.2013.08.019
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.345
IUBMB Enzyme Nomenclature: 1.1.1.345
ExPASy - ENZYME nomenclature database: 1.1.1.345
BRENDA, the Enzyme Database: 1.1.1.345

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