Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.37 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)

Crystallization (Comment) Organism
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]

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

Organism

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

Substrates and Products (Substrate)

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

Cofactor

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