Activating Compound | Comment | Organism | Structure |
---|---|---|---|
D-fructose 1,6-bisphosphate | activates | Methanocaldococcus jannaschii |
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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Methanocaldococcus jannaschii | Q60176 | - |
- |
Methanocaldococcus jannaschii DSM 2661 | Q60176 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Methanocaldococcus jannaschii |
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 | Comment | Organism |
---|---|---|
tetramer | exists in solution predominantly as a tetramer | Methanocaldococcus jannaschii |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
assay at | Methanocaldococcus jannaschii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 7 | assay at | Methanocaldococcus jannaschii |
6.6 | - |
assay at | Methanocaldococcus jannaschii |
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 |