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Literature summary extracted from

  • Tomita, T.; Fushinobu, S.; Kuzuyama, T.; Nishiyama, M.
    Structural basis for the alteration of coenzyme specificity in a malate dehydrogenase mutant (2006), Biochem. Biophys. Res. Commun., 347, 502-508.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.37 mutant EX7 (with altered coenzyme specificity from NADH towards NADPH) in complex with NADPH or NADH, 2.0 A resolution Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.37 0.0024
-
 NADH 30°C, pH 7.0, wild-type enzyme Thermus thermophilus
1.1.1.37 0.003
-
 oxaloacetate 30°C, pH 7.0, wild-type enzyme, cofactor NADH Thermus thermophilus
1.1.1.37 0.0426
-
 NADPH 30°C, pH 7.0, wild-type enzyme Thermus thermophilus
1.1.1.37 0.74
-
 oxaloacetate 30°C, pH 7.0, wild-type enzyme, cofactor NADPH Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.37 Thermus thermophilus P10584 wild-type enzyme and mutant EX7 (with altered coenzyme specificity from NADH towards NADPH)
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.37 oxaloacetate + NADPH + H+
-
 Thermus thermophilus (S)-malate + NADP+
-
 r

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.37 NADH
-
 Thermus thermophilus
1.1.1.37 NADPH mutant EX7 with altered coenzyme specificity from NADH towards NADPH Thermus thermophilus