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Literature summary extracted from
- Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea (2000), J. Bacteriol., 182, 3688-3692.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.1.337 | expression in Escherichia coli | Methanocaldococcus jannaschii |
| 1.1.1.337 | expression in Escherichia coli | Methanothermus fervidus |
| 1.1.1.375 | overexpressed in Escherichia coli | Methanocaldococcus jannaschii |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.337 | 0.04 | - |
3-sulfopyruvate | cosubstrate NADH, pH 8.0, 70°C | Methanocaldococcus jannaschii |  |
| 1.1.1.337 | 0.07 | - |
3-sulfopyruvate | cosubstrate NADH, pH 8.0, 70°C | Methanothermus fervidus | |
| 1.1.1.337 | 0.11 | - |
oxaloacetate | cosubstrate NADH, pH 8.0, 70°C | Methanothermus fervidus | |
| 1.1.1.337 | 0.13 | - |
oxaloacetate | cosubstrate NADH, pH 8.0, 70°C | Methanocaldococcus jannaschii | |
| 1.1.1.337 | 0.21 | - |
3-sulfopyruvate | cosubstrate NADPH, pH 8.0, 70°C | Methanocaldococcus jannaschii | |
| 1.1.1.337 | 0.21 | - |
3-sulfopyruvate | cosubstrate NADPH, pH 8.0, 70°C | Methanothermus fervidus | |
| 1.1.1.337 | 0.95 | - |
oxaloacetate | cosubstrate NADPH, pH 8.0, 70°C | Methanothermus fervidus | |
| 1.1.1.337 | 1.9 | - |
2-oxoglutarate | cosubstrate NADH, pH 8.0, 70°C | Methanocaldococcus jannaschii | |
| 1.1.1.337 | 5.32 | - |
oxaloacetate | cosubstrate NADPH, pH 8.0, 70°C | Methanocaldococcus jannaschii | |
| 1.1.1.337 | 15 | - |
1-oxo-1,3,4,6-hexanetetracarboxylate | cosubstrate NADH, pH 8.0, 70°C | Methanocaldococcus jannaschii | |
| 1.1.1.375 | 0.025 | - |
(S)-malate | 70°C, pH 9.5, cofactor: NADP+ | Methanocaldococcus jannaschii | |
| 1.1.1.375 | 0.15 | - |
(S)-malate | 70°C, pH 9.5, cofactor: NAD+ | Methanocaldococcus jannaschii | |
| 1.1.1.375 | 0.19 | - |
3-sulfopyruvate | 70°C, pH 8.0, cofactor: NADPH | Methanocaldococcus jannaschii | |
| 1.1.1.375 | 0.25 | - |
oxaloacetate | 70°C, pH 8.0, cofactor: NADH | Methanocaldococcus jannaschii | |
| 1.1.1.375 | 0.3 | - |
oxaloacetate | 70°C, pH 8.0, cofactor: NADPH | Methanocaldococcus jannaschii | |
| 1.1.1.375 | 1.3 | - |
3-sulfopyruvate | 70°C, pH 8.0, cofactor: NADH | Methanocaldococcus jannaschii | |
| 1.1.1.375 | 4.6 | - |
(2S)-3-sulfolactate | 70°C, pH 9.5, cofactor: NADP+ | Methanocaldococcus jannaschii | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.375 | 3-sulfopyruvate + NADPH + H+ | Methanocaldococcus jannaschii | - |
(2S)-3-sulfolactate + NADP+ | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.337 | Methanocaldococcus jannaschii | Q58820 | - |
- |
| 1.1.1.337 | Methanothermus fervidus | P16142 | - |
- |
| 1.1.1.375 | Methanocaldococcus jannaschii | Q60176 | - |
- |
| 1.1.1.375 | Methanocaldococcus jannaschii DSM 2661 | Q60176 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.337 | (2R)-3-sulfolactate + NAD+ | - |
Methanocaldococcus jannaschii | 3-sulfopyruvate + NADH + H+ | - |
r | |
| 1.1.1.337 | (2R)-3-sulfolactate + NAD+ | - |
Methanothermus fervidus | 3-sulfopyruvate + NADH + H+ | - |
r | |
| 1.1.1.337 | (S)-2-hydroxyglutarate + NAD+ | - |
Methanocaldococcus jannaschii | 2-oxoglutarate + NADH + H+ | - |
r | |
| 1.1.1.337 | (S)-lactate + NAD+ | - |
Methanocaldococcus jannaschii | pyruvate + NADH + H+ | - |
r | |
| 1.1.1.337 | (S)-lactate + NAD+ | - |
Methanothermus fervidus | pyruvate + NADH + H+ | - |
r | |
| 1.1.1.337 | 1-hydroxy-1,3,4,6-hexanetetracarboxylate + NAD+ | - |
Methanocaldococcus jannaschii | 1-oxo-1,3,4,6-hexanetetracarboxylate + NADH + H+ | - |
r | |
| 1.1.1.337 | 3-sulfopyruvate + NADH + H+ | - |
Methanocaldococcus jannaschii | (S)-3-sulfolactate + NAD+ | - |
r | |
| 1.1.1.337 | 3-sulfopyruvate + NADH + H+ | - |
Methanothermus fervidus | (S)-3-sulfolactate + NAD+ | - |
r | |
| 1.1.1.337 | 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 | ? | - |
? | |
| 1.1.1.337 | 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 | ? | - |
? | |
| 1.1.1.337 | oxaloacetate + NADH + H+ | - |
Methanocaldococcus jannaschii | (S)-malate + NAD+ | - |
? | |
| 1.1.1.337 | oxaloacetate + NADH + H+ | - |
Methanothermus fervidus | (S)-malate + NAD+ | - |
? | |
| 1.1.1.375 | (2S)-3-sulfolactate + NADP+ | weak activity, Vmax/KM: 1/min*mg. The enzyme does not catalyse the oxidation of (2S)-3-sulfolactate with NAD+ as cofactor | Methanocaldococcus jannaschii | 3-sulfopyruvate + NADPH + H+ | - |
r | |
| 1.1.1.375 | (S)-malate + NAD+ | Vmax/KM: 4/min*mg. The enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate | Methanocaldococcus jannaschii | oxaloacetate + NADH + H+ | - |
r | |
| 1.1.1.375 | (S)-malate + NAD+ | Vmax/KM: 4/min*mg. The enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate | Methanocaldococcus jannaschii DSM 2661 | oxaloacetate + NADH + H+ | - |
r | |
| 1.1.1.375 | (S)-malate + NADP+ | Vmax/KM: 110/min*mg. The enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate | Methanocaldococcus jannaschii | oxaloacetate + NADPH + H+ | - |
r | |
| 1.1.1.375 | (S)-malate + NADP+ | Vmax/KM: 110/min*mg. The enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate | Methanocaldococcus jannaschii DSM 2661 | oxaloacetate + NADPH + H+ | - |
r | |
| 1.1.1.375 | 3-sulfopyruvate + NADH + H+ | Vmax/KM: 34/min*mg. The enzyme prefers oxaloacetate over 3-sulfopyruvate using NADH as cofactor | Methanocaldococcus jannaschii | (2S)-3-sulfolactate + NAD+ | - |
ir | |
| 1.1.1.375 | 3-sulfopyruvate + NADPH + H+ | - |
Methanocaldococcus jannaschii | (2S)-3-sulfolactate + NADP+ | - |
r | |
| 1.1.1.375 | 3-sulfopyruvate + NADPH + H+ | Vmax/KM: 590/min*mg. The enzyme prefers NADPH over NADH in reduction of 3-sulfopyruvate | Methanocaldococcus jannaschii | (2S)-3-sulfolactate + NADP+ | - |
r | |
| 1.1.1.375 | additional information | no activity with 2-oxoglutarate and 1-oxo-1,3,4,6-hexanetetracarboxylic acid | Methanocaldococcus jannaschii | ? | - |
? | |
| 1.1.1.375 | additional information | no activity with 2-oxoglutarate and 1-oxo-1,3,4,6-hexanetetracarboxylic acid | Methanocaldococcus jannaschii DSM 2661 | ? | - |
? | |
| 1.1.1.375 | oxaloacetate + NADH + H+ | Vmax/KM: 120 /min*mg. The enzyme prefers oxaloacetate over 3-sulfopyruvate using NADH as cofactor. The enzyme prefers NADPH over NADH in reduction of oxaloacetate | Methanocaldococcus jannaschii | (S)-malate + NAD+ | - |
r | |
| 1.1.1.375 | oxaloacetate + NADH + H+ | Vmax/KM: 120 /min*mg. The enzyme prefers oxaloacetate over 3-sulfopyruvate using NADH as cofactor. The enzyme prefers NADPH over NADH in reduction of oxaloacetate | Methanocaldococcus jannaschii DSM 2661 | (S)-malate + NAD+ | - |
r | |
| 1.1.1.375 | oxaloacetate + NADPH + H+ | Vmax/KM: 160/min*mg. The enzyme prefers NADPH over NADH in reduction of oxaloacetate | Methanocaldococcus jannaschii | (S)-malate + NADP+ | - |
r | |
| 1.1.1.375 | oxaloacetate + NADPH + H+ | Vmax/KM: 160/min*mg. The enzyme prefers NADPH over NADH in reduction of oxaloacetate | Methanocaldococcus jannaschii DSM 2661 | (S)-malate + NADP+ | - |
r | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.337 | MJ1425 | - |
Methanocaldococcus jannaschii |
| 1.1.1.337 | MJ1425 | - |
Methanothermus fervidus |
| 1.1.1.375 | MdhII | - |
Methanocaldococcus jannaschii |
| 1.1.1.375 | MJ0490 | locus name | Methanocaldococcus jannaschii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.375 | 70 | - |
assay at | Methanocaldococcus jannaschii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.337 | NADH | - |
Methanothermus fervidus | |
| 1.1.1.337 | NADH | ratio vmax/Km for NADH is about 20fold greater than for NADPH | Methanocaldococcus jannaschii | |
| 1.1.1.337 | NADPH | - |
Methanothermus fervidus | |
| 1.1.1.337 | NADPH | ratio vmax/Km for NADH is about 20fold greater than for NADPH | Methanocaldococcus jannaschii | |
| 1.1.1.375 | NAD+ | the enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate | Methanocaldococcus jannaschii | |
| 1.1.1.375 | NADH | the enzyme prefers NADPH over NADH in reduction of oxaloacetate | Methanocaldococcus jannaschii | |
| 1.1.1.375 | NADP+ | the enzyme prefers NADP+ over NAD+ in oxidation of (S)-malate | Methanocaldococcus jannaschii | |
| 1.1.1.375 | NADPH | the enzyme prefers NADPH over NADH in reduction of oxaloacetate or 3-sulfopyruvate | Methanocaldococcus jannaschii | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.1.1.337 | physiological function | enzyme is likely to be involved in the biosynthesis of both coenzyme M and methanopterin | Methanocaldococcus jannaschii |
| 1.1.1.337 | physiological function | enzyme is likely to be involved in the biosynthesis of both coenzyme M and methanopterin | Methanothermus fervidus |
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