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Literature summary extracted from

  • Graczer, E.; Lionne, C.; Zavodszky, P.; Chaloin, L.; Vas, M.
    Transient kinetic studies reveal isomerization steps along the kinetic pathway of Thermus thermophilus 3-isopropylmalate dehydrogenase (2013), FEBS J., 280, 1764-1772.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.85 0.013
-
(2R,3S)-3-isopropylmalate pH 7.6, 20°C, stopped flow experiment Thermus thermophilus
1.1.1.85 0.25
-
NAD+ pH 7.6, 20°C, stopped flow experiment Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.85 Thermus thermophilus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.85 (2R,3S)-3-isopropylmalate + NAD+
-
Thermus thermophilus 2-oxoisocaproate + NADH + H+ + CO2
-
?
1.1.1.85 additional information reaction scheme based on incorporation of the rate constant of a fast protein conformational change such as domain closure derived from the separately recorded time-dependent formation of the fluorescence resonance energy transfer signal. The rate-limiting step seems to be another slower conformational change that allows product release Thermus thermophilus ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.85 2.9
-
(2R,3S)-3-isopropylmalate pH 7.6, 20°C, quenched flow experiment Thermus thermophilus
1.1.1.85 3.4
-
(2R,3S)-3-isopropylmalate pH 7.6, 20°C, stopped flow experiment Thermus thermophilus