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Information on EC 1.1.1.337 - L-2-hydroxycarboxylate dehydrogenase (NAD+) and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58820

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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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Methanocaldococcus jannaschii
UNIPROT: Q58820
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
l-hicdh, l-2-hydroxyisocaproate dehydrogenase, sulfolactate dehydrogenase, mj1425, mdh i, l-hydroxyisocaproate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(R)-sulfolactate dehydrogenase
-
-
-
-
ComC
-
-
-
-
L-2-hydroxyacid dehydrogenase (NAD+)
-
-
-
-
L-sulfolactate dehydrogenase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
-
-
-
r
(S)-2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-lactate + NAD+
pyruvate + NADH + H+
show the reaction diagram
-
-
-
r
1-hydroxy-1,3,4,6-hexanetetracarboxylate + NAD+
1-oxo-1,3,4,6-hexanetetracarboxylate + NADH + H+
show the reaction diagram
-
-
-
r
2-oxoglutarate + NADH + H+
(S)-2-hydroxyglutarate + NAD+
show the reaction diagram
-
-
-
?
2-oxopentanedioic acid + NADH + H+
2-hydroxypentandioic acid + NAD+
show the reaction diagram
-
-
-
?
3-sulfopyruvate + NADH + H+
(S)-3-sulfolactate + NAD+
show the reaction diagram
-
-
-
r
3-sulfopyruvate + NADH + H+
3-sulfolactate + NAD+
show the reaction diagram
-
-
-
?
glyoxylate + NADH + H+
2-hydroxypropanoate + NAD+
show the reaction diagram
-
-
-
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
show the reaction diagram
oxaloacetate + NADH + H+
malate + NAD+
show the reaction diagram
-
-
-
?
oxopropandioic acid + NADH + H+
2-hydroxypropanedioic acid + NAD+
show the reaction diagram
-
-
-
?
pyruvate + NADH + H+
(S)-lactate + NAD+
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
ratio vmax/Km for NADH is about 20fold greater than for NADPH
NADPH
ratio vmax/Km for NADH is about 20fold greater than for NADPH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
1-oxo-1,3,4,6-hexanetetracarboxylate
cosubstrate NADH, pH 8.0, 70°C
1.9
2-oxoglutarate
cosubstrate NADH, pH 8.0, 70°C
1.9
2-oxopentanedioic acid
pH 8.0, 70°C
0.04 - 0.21
3-sulfopyruvate
46
glyoxylate
pH 8.0, 70°C
0.13 - 5.32
oxaloacetate
3.4
oxopropandioic acid
pH 8.0, 70°C
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
gel filtration and velocity sedimentation data
75000
2 * 75000, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 75000, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with NADH, to 2.5 A resolution. The asymmetric unit contains a tetramer of tight dimers. Structure does not contain a cofactor-binding domain with Rossmann-fold topology. The NADH is bound in an extended conformation in each active site, in a manner that explains the pro-S specificity. Cofactor binding involves residues belonging to both subunits within the tight dimers. The results indicate the existence of a substrate discrimination mechanism, which involves electrostatic interactions
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
Irimia, A.; Madern, D.; Zaccai, G.; Vellieux, F.M.
Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes
EMBO J.
23
1234-1244
2004
Methanocaldococcus jannaschii (Q58820), Methanocaldococcus jannaschii
Manually annotated by BRENDA team