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Information on EC 1.1.1.337 - L-2-hydroxycarboxylate dehydrogenase (NAD+) and Organism(s) Methanothermus fervidus and UniProt Accession P16142

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IUBMB Comments
The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate . Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.
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This record set is specific for:
Methanothermus fervidus
UNIPROT: P16142
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Word Map
The taxonomic range for the selected organisms is: Methanothermus fervidus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
l-hicdh, l-2-hydroxyisocaproate dehydrogenase, sulfolactate dehydrogenase, mj1425, l-hydroxyisocaproate dehydrogenase, mdh i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(R)-sulfolactate dehydrogenase
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ComC
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-
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L-2-hydroxyacid dehydrogenase (NAD+)
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L-sulfolactate dehydrogenase
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
(2S)-2-hydroxycarboxylate:NAD+ oxidoreductase
The enzyme from the archaeon Methanocaldococcus jannaschii acts on multiple (S)-2-hydroxycarboxylates including (2R)-3-sulfolactate, (S)-malate, (S)-lactate, and (S)-2-hydroxyglutarate [3]. Note that (2R)-3-sulfolactate has the same stereo configuration as (2S)-2-hydroxycarboxylates.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-3-sulfolactate + NAD+
3-sulfopyruvate + NADH + H+
show the reaction diagram
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-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
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-
-
r
3-sulfopyruvate + NADH + H+
(S)-3-sulfolactate + NAD+
show the reaction diagram
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-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07 - 0.21
3-sulfopyruvate
0.11 - 0.95
oxaloacetate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme is likely to be involved in the biosynthesis of both coenzyme M and methanopterin
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Graupner, M.; Xu, H.; White, R.H.
Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea
J. Bacteriol.
182
3688-3692
2000
Methanocaldococcus jannaschii (Q58820), Methanocaldococcus jannaschii, Methanothermus fervidus (P16142), Methanothermus fervidus
Manually annotated by BRENDA team
Graupner, M.; White, R.H.
The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea
Biochim. Biophys. Acta
158
169-173
2001
Methanothermus fervidus (P16142), Methanocaldococcus jannaschii (Q58820)
Manually annotated by BRENDA team