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Literature summary for 1.1.1.375 extracted from
- Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases (2001), J. Mol. Biol., 307, 1351-1362.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| D-fructose 1,6-bisphosphate | activates | Methanocaldococcus jannaschii |  |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| determined in two crystal forms: a dimeric structure in the orthorhombic crystal at 1.9 A resolution and a tetrameric structure in the tetragonal crystal at 2.8 A | Methanocaldococcus jannaschii |
| the three-dimensional structure is determined in two crystal forms: a dimeric structure in the orthorhombic crystal at 1.9 A resolution and a structure in the tetragonal crystal at 2.8 A | Methanocaldococcus jannaschii |
| the three-dimensional structure of its gene product has been determined in two crystal forms: a dimeric structure in the orthorhombic crystal at 1.9 A resolution and a tetrameric structure in the tetragonal crystal at 2.8 A | Methanocaldococcus jannaschii |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.2 | - |
NADPH | pH 6.0-7.0, 45°C | Methanocaldococcus jannaschii | |
| 0.84 | - |
pyruvate | pH 6.0-7.0, 45°C | Methanocaldococcus jannaschii | |
| 0.84 | - |
pyruvate | pH 6.6, 45°C | Methanocaldococcus jannaschii | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanocaldococcus jannaschii | Q60176 | - |
- |
| Methanocaldococcus jannaschii DSM 2661 | Q60176 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Methanocaldococcus jannaschii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-sulfopyruvate + NADH | preference of NADPH over NADH | Methanocaldococcus jannaschii | (2R)-3-sulfolactate + NAD+ | - |
? | |
| 3-sulfopyruvate + NADH | preference of NADPH over NADH | Methanocaldococcus jannaschii DSM 2661 | (2R)-3-sulfolactate + NAD+ | - |
? | |
| 3-sulfopyruvate + NADPH | the reverse oxidation reaction occurs at least ten to 20 times more slowly. Preference of NADPH over NADH | Methanocaldococcus jannaschii | (2R)-3-sulfolactate + NADP+ | - |
? | |
| oxaloacetate + NADH | preference of NADPH over NADH | Methanocaldococcus jannaschii | (S)-malate + NAD+ | - |
r | |
| oxaloacetate + NADH | preference of NADPH over NADH | Methanocaldococcus jannaschii DSM 2661 | (S)-malate + NAD+ | - |
r | |
| oxaloacetate + NADPH | the reverse oxidation reaction occurs at least ten to 20 times more slowly. Preference of NADPH over NADH | Methanocaldococcus jannaschii | (S)-malate + NADP+ | - |
r | |
| oxaloacetate + NADPH | the reverse oxidation reaction occurs at least ten to 20 times more slowly. Preference of NADPH over NADH | Methanocaldococcus jannaschii DSM 2661 | (S)-malate + NADP+ | - |
r | |
| pyruvate + NADH | preference of NADPH over NADH. Activity is detected only when the allosteric activator fructose-1,6-bisphosphate is added to the assay mixture | Methanocaldococcus jannaschii | (S)-lactate + NAD+ | - |
? | |
| pyruvate + NADH + H+ | ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions | Methanocaldococcus jannaschii | (S)-lactate + NAD+ | - |
ir | |
| pyruvate + NADH + H+ | ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions | Methanocaldococcus jannaschii DSM 2661 | (S)-lactate + NAD+ | - |
ir | |
| pyruvate + NADPH | preference of NADPH over NADH. Activity is detected only when the allosteric activator fructose-1,6-bisphosphate is added to the assay mixture | Methanocaldococcus jannaschii | (S)-lactate + NADP+ | - |
? | |
| pyruvate + NADPH + H+ | ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions | Methanocaldococcus jannaschii | (S)-lactate + NADP+ | - |
ir | |
| pyruvate + NADPH + H+ | ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C (with 0.4 mM fructose 1,6-bisphosphate). The enzymatic activity for the oxidation reaction can not be measured under the tested conditions | Methanocaldococcus jannaschii DSM 2661 | (S)-lactate + NADP+ | - |
ir | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | exists in solution predominantly as a tetramer | Methanocaldococcus jannaschii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lactate/malate dehydrogenase | - |
Methanocaldococcus jannaschii |
| MdhII | - |
Methanocaldococcus jannaschii |
| MJ0409 | locus name | Methanocaldococcus jannaschii |
| MJ0490 | - |
Methanocaldococcus jannaschii |
| MJ0490 | locus name | Methanocaldococcus jannaschii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
assay at | Methanocaldococcus jannaschii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 7 | assay at | Methanocaldococcus jannaschii |
| 6.6 | - |
assay at | Methanocaldococcus jannaschii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD(P)H | the cofactor is bound at the active site | Methanocaldococcus jannaschii | |
| NAD+ | preference of NADP(H) over NAD(H). The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases | Methanocaldococcus jannaschii | |
| NADH | preference of NADP(H) over NAD(H).. The ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C. The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases | Methanocaldococcus jannaschii | |
| NADH | preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site | Methanocaldococcus jannaschii | |
| NADP+ | preference of NADP(H) over NAD(H). The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases | Methanocaldococcus jannaschii | |
| NADPH | preference of NADP(H) over NAD(H). The ratio of reaction rates for NADPH and NADH is 1.3-1.6 in the temperature range of 30-60°C. The cofactor preference is explained by the presence of a glycine residue in the cofactor binding pocket (Gly33), which replaces a conserved aspartate (or glutamate) residue in other NAD-dependent L-lactate dehydrogenases or malate dehydrogenases | Methanocaldococcus jannaschii | |
| NADPH | preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site | Methanocaldococcus jannaschii | |
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