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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.85 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.85 0.0022
-
 NAD+ pH 8.0, 25°C, wild-type enzyme Thermus thermophilus
1.1.1.85 0.012
-
 NAD+ pH 8.0, 40°C, wild-type enzyme Thermus thermophilus
1.1.1.85 0.21
-
 NAD+ pH 8.0, 70°C, wild-type enzyme Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.85 (2R,3S)-3-isopropylmalate + NAD+ Thermus thermophilus
-
 4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.85 Thermus thermophilus Q5SIY4
-
-

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 4-methyl-2-oxopentanoate + CO2 + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.85 homodimer
-
 Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.85 IPMDH
-
 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 0.37
-
 NAD+ pH 8.0, 25°C, wild-type enzyme Thermus thermophilus
1.1.1.85 2.4
-
 NAD+ pH 8.0, 40°C, wild-type enzyme Thermus thermophilus
1.1.1.85 79
-
 NAD+ pH 8.0, 70°C, wild-type enzyme Thermus thermophilus

General Information

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