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Literature summary for 1.1.1.337 extracted from

  • Graupner, M.; Xu, H.; White, R.H.
    Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea (2000), J. Bacteriol., 182, 3688-3692.
    View publication on PubMed
Search for more literature for 1.1.1.337

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Methanocaldococcus jannaschii
expression in Escherichia coli Methanothermus fervidus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
 3-sulfopyruvate cosubstrate NADH, pH 8.0, 70°C Methanocaldococcus jannaschii
0.07
-
 3-sulfopyruvate cosubstrate NADH, pH 8.0, 70°C Methanothermus fervidus
0.11
-
 oxaloacetate cosubstrate NADH, pH 8.0, 70°C Methanothermus fervidus
0.13
-
 oxaloacetate cosubstrate NADH, pH 8.0, 70°C Methanocaldococcus jannaschii
0.21
-
 3-sulfopyruvate cosubstrate NADPH, pH 8.0, 70°C Methanocaldococcus jannaschii
0.21
-
 3-sulfopyruvate cosubstrate NADPH, pH 8.0, 70°C Methanothermus fervidus
0.95
-
 oxaloacetate cosubstrate NADPH, pH 8.0, 70°C Methanothermus fervidus
1.9
-
 2-oxoglutarate cosubstrate NADH, pH 8.0, 70°C Methanocaldococcus jannaschii
5.32
-
 oxaloacetate cosubstrate NADPH, pH 8.0, 70°C Methanocaldococcus jannaschii
15
-
 1-oxo-1,3,4,6-hexanetetracarboxylate cosubstrate NADH, pH 8.0, 70°C Methanocaldococcus jannaschii

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58820
-
-
Methanothermus fervidus P16142
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2R)-3-sulfolactate + NAD+
-
 Methanocaldococcus jannaschii 3-sulfopyruvate + NADH + H+
-
 r
(2R)-3-sulfolactate + NAD+
-
 Methanothermus fervidus 3-sulfopyruvate + NADH + H+
-
 r
(S)-2-hydroxyglutarate + NAD+
-
 Methanocaldococcus jannaschii 2-oxoglutarate + NADH + H+
-
 r
(S)-lactate + NAD+
-
 Methanocaldococcus jannaschii pyruvate + NADH + H+
-
 r
(S)-lactate + NAD+
-
 Methanothermus fervidus pyruvate + NADH + H+
-
 r
1-hydroxy-1,3,4,6-hexanetetracarboxylate + NAD+
-
 Methanocaldococcus jannaschii 1-oxo-1,3,4,6-hexanetetracarboxylate + NADH + H+
-
 r
3-sulfopyruvate + NADH + H+
-
 Methanocaldococcus jannaschii (S)-3-sulfolactate + NAD+
-
 r
3-sulfopyruvate + NADH + H+
-
 Methanothermus fervidus (S)-3-sulfolactate + NAD+
-
 r
additional information enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: pyruvate Methanocaldococcus jannaschii ?
-
 ?
additional information enzyme additionally functions as malate dehydrogenase, reducing oxalacetate to (S)-malate using either NADH or NADPH as a reductant. No substrate: 2-oxoglutarate, pyruvate, 1-oxo-1,3,4,6-hexanetetracarboxylate Methanothermus fervidus ?
-
 ?
oxaloacetate + NADH + H+
-
 Methanocaldococcus jannaschii (S)-malate + NAD+
-
 ?
oxaloacetate + NADH + H+
-
 Methanothermus fervidus (S)-malate + NAD+
-
 ?

Synonyms

Synonyms Comment Organism
MJ1425
-
 Methanocaldococcus jannaschii
MJ1425
-
 Methanothermus fervidus

Cofactor

Cofactor Comment Organism Structure
NADH ratio vmax/Km for NADH is about 20fold greater than for NADPH Methanocaldococcus jannaschii
NADH
-
 Methanothermus fervidus
NADPH ratio vmax/Km for NADH is about 20fold greater than for NADPH Methanocaldococcus jannaschii
NADPH
-
 Methanothermus fervidus

General Information

General Information Comment Organism
physiological function enzyme is likely to be involved in the biosynthesis of both coenzyme M and methanopterin Methanocaldococcus jannaschii
physiological function enzyme is likely to be involved in the biosynthesis of both coenzyme M and methanopterin Methanothermus fervidus