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Literature summary for 1.1.1.85 extracted from

  • Moriyma, H.; Onodera, K.; Sakurai, M.; Tanaka, N.; Kirino-Kagawa, H.; Oshima, T.; Katsube, Y.
    The crystal structures of mutated 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8 and their relationship to the thermostability of the enzyme (1995), J. Biochem., 117(2), 408-413.
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Crystallization (Commentary)

Crystallization (Comment) Organism
study of the mutant enzymes G240A and L246E/V249M by X-ray crystallography Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
G240A decreased thermostability Thermus thermophilus
L246E/V249M decreased thermostability Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2R,3S)-3-isopropylmalate + NAD+
-
 Thermus thermophilus 2-oxoisocaproate + NADH + H+ + CO2
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
87
-
 the extended hydrogen bonds within the beta-sheet are the major reason for the decreased thermostability of G240A Thermus thermophilus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Thermus thermophilus