Literature summary for 1.1.1.85 extracted from

Aoshima, M.; Oshima, T.
Stabilization of Escherichia coli isopropylmalate dehydrogenase by single amino acid substitution (1997), Protein Eng., 10, 249-254.

Search for more literature for 1.1.1.85

Cloned(Commentary)

Cloned (Comment)	Organism
the sequence motif is introduced into a mesophilic Escherichia coli isopropylmalate dehydrogenase, one by one. The introduction of the whole motif leads the mesophilic enzyme to be more unstable whereas substitution of only one amino acid residue in the motif thermostabilizes the enzyme	Thermus thermophilus

Protein Variants

Protein Variants	Comment	Organism
L204F	higher thermostability compared to wild-type enzyme, denaturation rates at 68°C and 70°C are slower	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	key enzyme in leucine biosynthesis	2-oxoisocaproate + NADH + H+ + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Thermus thermophilus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
gene cloned in Escherichia coli	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	-	?
(2R,3S)-3-isopropylmalate + NAD+	-	Escherichia coli	2-oxoisocaproate + NADH + H+ + CO2	-	?
(2R,3S)-3-isopropylmalate + NAD+	key enzyme in leucine biosynthesis	Thermus thermophilus	2-oxoisocaproate + NADH + H+ + CO2	-	?

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	mutant enzyme L204F shows higher thermostability compared to wild-type enzyme, denaturation rates at 68°C and 70°C are slower for the mutant enzyme than for wild-type enzyme	Thermus thermophilus
87	-	the thermophilic IMPDH was succesfully stabilized by replacing Ala172 with more hydrophobic residues like Glu, Asn and Gln without significant change in the enzymatic activity	Thermus thermophilus

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Thermus thermophilus
NAD+	-	Escherichia coli

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Release 2023.1 (January 2023)