EC number:1.1.1.337

Enzyme

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     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.1 With NAD+ or NADP+ as acceptor
ID:1.1.1.337
Description:L-2-hydroxycarboxylate dehydrogenase (NAD(+)).
Alternative Name: L-sulfolactate dehydrogenase.
L-2-hydroxyacid dehydrogenase (NAD(+)).
(R)-sulfolactate dehydrogenase.
Cath: 1.10.1530.10; 3.30.1370.60; 3.40.50.720; 3.90.110.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.1.337
BRENDA Enzyme Link: BRENDA 1.1.1.337
KEGG Enzyme Link: KEGG1.1.1.337
BioCyc Enzyme Link: BioCyc 1.1.1.337
ExPASy Enzyme Link: ExPASy1.1.1.337
EC2PDB Enzyme Link: EC2PDB 1.1.1.337
ExplorEnz Enzyme Link: ExplorEnz 1.1.1.337
PRIAM enzyme-specific profiles Link: PRIAM 1.1.1.337
IntEnz Enzyme Link: IntEnz 1.1.1.337
MEDLINE Enzyme Link: MEDLINE 1.1.1.337

EC number:1.1.1.337

MSA:

1.1.1.337;
Phylogenetic Tree:

1.1.1.337;
Uniprot:
M-CSA:
RHEA:34555 a (2S)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1
Reaction
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References

TitleAuthorsDatePubMed ID
Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix.Kawakami R, Sakuraba H, Goda S, Tsuge H, Ohshima T2009 Oct19555779
The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea.Graupner M, White RH2001 Jul 911451450
The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase.Madern D2000 Sep10998181
Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea.Graupner M, Xu H, White RH2000 Jul10850983
Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA.Rein U, Gueta R, Denger K, Ruff J, Hollemeyer K, Cook AM2005 Mar15758220
Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics.Graham DE, White RH2002 Apr12013276