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Literature summary for 1.1.1.85 extracted from

  • Akanuma, S.; Bessho, M.; Kimura, H.; Furukawa, R.; Yokobori, S.; Yamagishi, A.
    Establishment of mesophilic-like catalytic properties in a thermophilic enzyme without affecting its thermal stability (2019), Sci. Rep., 9, 9346 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
tertiary structure solved by X-ray crystallography at 2.2 A resolution Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
additional information one or a combination of amino acid(s) in 3-isopropylmalate dehydrogenase is/are substituted by a residue(s) found in the Escherichia coli enzyme at the same position(s). The best mutant, which contains three amino acid substitutions, shows a 17fold higher specific activity at 25°C compared to the original wild-type enzyme while retaining high thermal stability. The kinetic and thermodynamic parameters of the mutant show similar patterns along the reaction coordinate to those of the mesophilic enzyme Thermus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0022
-
NAD+ pH 8.0, 25°C, wild-type enzyme Thermus thermophilus
0.012
-
NAD+ pH 8.0, 40°C, wild-type enzyme Thermus thermophilus
0.21
-
NAD+ pH 8.0, 70°C, wild-type enzyme Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2R,3S)-3-isopropylmalate + NAD+ Thermus thermophilus
-
4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q5SIY4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2R,3S)-3-isopropylmalate + NAD+
-
Thermus thermophilus 4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
?

Subunits

Subunits Comment Organism
homodimer
-
Thermus thermophilus

Synonyms

Synonyms Comment Organism
IPMDH
-
Thermus thermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.37
-
NAD+ pH 8.0, 25°C, wild-type enzyme Thermus thermophilus
2.4
-
NAD+ pH 8.0, 40°C, wild-type enzyme Thermus thermophilus
79
-
NAD+ pH 8.0, 70°C, wild-type enzyme Thermus thermophilus

General Information

General Information Comment Organism
physiological function the enzyme is involved in the third step of the leucine biosynthesis pathway Thermus thermophilus