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Literature summary extracted from

  • Madern, D.
    The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase (2000), Mol. Microbiol., 37, 1515-1520.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.375 oxaloacetate above 0.3 mM Methanocaldococcus jannaschii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.375 0.02
-
 NADPH 70°C, pH 8.0 Methanocaldococcus jannaschii
1.1.1.375 0.06
-
 oxaloacetate 70°C, pH 8.0 Methanocaldococcus jannaschii
1.1.1.375 0.14
-
 NADH 70°C, pH 8.0 Methanocaldococcus jannaschii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.375 Ca2+ in the presence of NADPH, 10 mM MgCl2, MnCl2 or CaCl2 is required to support full activity. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration Methanocaldococcus jannaschii
1.1.1.375 K+ in the presence of NADPH, full enzymatic activity requires a minimum salt concentration of 0.1 M NaCl or KCl. At lower salt concentrations, the activity decreases by a factor of three. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration Methanocaldococcus jannaschii
1.1.1.375 Mg2+ in the presence of NADPH, 10 mM MgCl2, MnCl2 or CaCl2 is required to support full activity. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration Methanocaldococcus jannaschii
1.1.1.375 Mn2+ in the presence of NADPH, 10 mM MgCl2, MnCl2 or CaCl2 is required to support full activity. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration Methanocaldococcus jannaschii
1.1.1.375 Na+ in the presence of NADPH, full enzymatic activity requires a minimum salt concentration of 0.1 M NaCl or KCl. At lower salt concentrations, the activity decreases by a factor of three. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration Methanocaldococcus jannaschii

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.1.1.375 guanidine-HCl transition between folded and unfolded enzyme (monitored by the change in molar ellipticity at 222 nm) is found at 2 M guanidine hydrochloride 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
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.1.1.375 the enzyme is not sensitive to oxygen Methanocaldococcus jannaschii

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 oxaloacetate + NADH + H+
-
 Methanocaldococcus jannaschii (S)-malate + NAD+
-
 r
1.1.1.375 oxaloacetate + NADH + H+
-
 Methanocaldococcus jannaschii DSM 2661 (S)-malate + NAD+
-
 r
1.1.1.375 oxaloacetate + NADPH + H+
-
 Methanocaldococcus jannaschii (S)-malate + NADP+
-
 r
1.1.1.375 oxaloacetate + NADPH + H+
-
 Methanocaldococcus jannaschii DSM 2661 (S)-malate + NADP+
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.375 MJ0409 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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.375 80
-
 thermal transition between active and inactive enzyme starts at about 80°C and follows first-order kinetics Methanocaldococcus jannaschii

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.375 NADH NADPH is the preferred coenzyme Methanocaldococcus jannaschii
1.1.1.375 NADPH NADPH is the preferred coenzyme Methanocaldococcus jannaschii