KEGG   ENZYME: 1.1.1.375
Entry
EC 1.1.1.375                Enzyme                                 
Name
L-2-hydroxycarboxylate dehydrogenase [NAD(P)+];
MdhII;
lactate/malate dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
(2S)-2-hydroxycarboxylate:NAD(P)+ oxidoreductase
Reaction(IUBMB)
a (2S)-2-hydroxycarboxylate + NAD(P)+ = a 2-oxocarboxylate + NAD(P)H + H+ [RN:R10189 R10786]
Reaction(KEGG)
R10189 R10786
Substrate
(2S)-2-hydroxycarboxylate [CPD:C15565];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Product
2-oxocarboxylate [CPD:C00161];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
The enzyme from the archaeon Methanocaldococcus jannaschii catalyses the reversible oxidation of (2R)-3-sulfolactate and (S)-malate to 3-sulfopyruvate and oxaloacetate, respectively (note that (2R)-3-sulfolactate has the same stereochemical configuration as (2S)-2-hydroxycarboxylates) [1]. The enzyme can use both NADH and NADPH, although activity is higher with NADPH [1-3]. The oxidation of (2R)-3-sulfolactate was observed only in the presence of NADP+ [1]. The same organism also possesses an NAD+-specific enzyme with similar activity, cf. EC 1.1.1.337, L-2-hydroxycarboxylate dehydrogenase (NAD+).
History
EC 1.1.1.375 created 2014
Reference
1  [PMID:10850983]
  Authors
Graupner M, Xu H, White RH
  Title
Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea.
  Journal
J Bacteriol 182:3688-92 (2000)
DOI:10.1128/JB.182.13.3688-3692.2000
  Sequence
[mja:MJ_0490]
Reference
2  [PMID:11292347]
  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.
  Journal
J Mol Biol 307:1351-62 (2001)
DOI:10.1006/jmbi.2001.4532
  Sequence
[mja:MJ_0490]
Reference
3  [PMID:10998181]
  Authors
Madern D
  Title
The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase.
  Journal
Mol Microbiol 37:1515-20 (2000)
DOI:10.1046/j.1365-2958.2000.02113.x
  Sequence
[mja:MJ_0490]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.375
IUBMB Enzyme Nomenclature: 1.1.1.375
ExPASy - ENZYME nomenclature database: 1.1.1.375
BRENDA, the Enzyme Database: 1.1.1.375

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Chemical substance (7)   
   KEGG COMPOUND (7)   
Chemical reaction (3)   
   KEGG REACTION (2)   
   KEGG RCLASS (1)   
Protein sequence (11)   
   UniProt (4)   
   SWISS-PROT (1)   
   RefSeq(pep) (6)   
DNA sequence (10)   
   RefSeq(nuc) (6)   
   GenBank (2)   
   EMBL (2)   
Protein domain (6)   
   InterPro (6)   
All databases (37)   

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