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Literature summary extracted from

  • Lee, B.I.; Chang, C.; Cho, S.J.; Eom, S.H.; Kim, K.K.; Yu, Y.G.; Suh, S.W.
    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.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.375 D-fructose 1,6-bisphosphate activates Methanocaldococcus jannaschii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.375 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
1.1.1.375 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
1.1.1.375 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.375 0.2
-
 NADPH pH 6.0-7.0, 45°C Methanocaldococcus jannaschii
1.1.1.375 0.84
-
 pyruvate pH 6.0-7.0, 45°C Methanocaldococcus jannaschii
1.1.1.375 0.84
-
 pyruvate pH 6.6, 45°C Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.375 Methanocaldococcus jannaschii Q60176
-
-
1.1.1.375 Methanocaldococcus jannaschii DSM 2661 Q60176
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.375
-
 Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.375 3-sulfopyruvate + NADH preference of NADPH over NADH Methanocaldococcus jannaschii (2R)-3-sulfolactate + NAD+
-
 ?
1.1.1.375 3-sulfopyruvate + NADH preference of NADPH over NADH Methanocaldococcus jannaschii DSM 2661 (2R)-3-sulfolactate + NAD+
-
 ?
1.1.1.375 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+
-
 ?
1.1.1.375 oxaloacetate + NADH preference of NADPH over NADH Methanocaldococcus jannaschii (S)-malate + NAD+
-
 r
1.1.1.375 oxaloacetate + NADH preference of NADPH over NADH Methanocaldococcus jannaschii DSM 2661 (S)-malate + NAD+
-
 r
1.1.1.375 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
1.1.1.375 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
1.1.1.375 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+
-
 ?
1.1.1.375 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
1.1.1.375 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
1.1.1.375 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+
-
 ?
1.1.1.375 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
1.1.1.375 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

EC Number Subunits Comment Organism
1.1.1.375 tetramer exists in solution predominantly as a tetramer Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
1.1.1.375 lactate/malate dehydrogenase
-
 Methanocaldococcus jannaschii
1.1.1.375 MdhII
-
 Methanocaldococcus jannaschii
1.1.1.375 MJ0409 locus name Methanocaldococcus jannaschii
1.1.1.375 MJ0490
-
 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 45
-
 assay at Methanocaldococcus jannaschii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.375 6 7 assay at Methanocaldococcus jannaschii
1.1.1.375 6.6
-
 assay at Methanocaldococcus jannaschii

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.375 NAD(P)H the cofactor is bound at the active site Methanocaldococcus jannaschii
1.1.1.375 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
1.1.1.375 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
1.1.1.375 NADH preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site Methanocaldococcus jannaschii
1.1.1.375 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
1.1.1.375 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
1.1.1.375 NADPH preference of NADPH over NADH. The cofactor NADP(H) is bound at the active site Methanocaldococcus jannaschii