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Literature summary for 1.1.1.375 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
Search for more literature for 1.1.1.375

Inhibitors

Inhibitors Comment Organism Structure
oxaloacetate above 0.3 mM Methanocaldococcus jannaschii

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
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
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
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
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

Organic Solvent Comment Organism
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

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q60176
-
-
Methanocaldococcus jannaschii DSM 2661 Q60176
-
-

Oxidation Stability

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

Purification (Commentary)

Purification (Comment) Organism
-
 Methanocaldococcus jannaschii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxaloacetate + NADH + H+
-
 Methanocaldococcus jannaschii (S)-malate + NAD+
-
 r
oxaloacetate + NADH + H+
-
 Methanocaldococcus jannaschii DSM 2661 (S)-malate + NAD+
-
 r
oxaloacetate + NADPH + H+
-
 Methanocaldococcus jannaschii (S)-malate + NADP+
-
 r
oxaloacetate + NADPH + H+
-
 Methanocaldococcus jannaschii DSM 2661 (S)-malate + NADP+
-
 r

Synonyms

Synonyms Comment Organism
MJ0409 locus name Methanocaldococcus jannaschii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
 assay at Methanocaldococcus jannaschii

Temperature Stability [°C]

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

Cofactor

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