Literature summary for 1.1.1.85 extracted from

Imada, K.; Inagaki, K.; Matsunami, H.; Kawaguchi, H.; Tanaka, H.; Tanaka, N.; Namba, K.
Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism (1998), Structure, 6, 971-982.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme in complex with 3-isopropylmalate	Acidithiobacillus ferrooxidans

Organism

Organism	UniProt	Comment	Textmining
Acidithiobacillus ferrooxidans	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(2R,3S)-3-isopropylmalate + NAD+	a large movement of domain 1 is induced by substrate binding, which results in the formation of the hydrophobic pocket for the gamma-isopropyl moiety of isopropylmalate	Acidithiobacillus ferrooxidans	2-oxoisocaproate + NADH + H+ + CO2	-	?

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	the acidic tip of IPM-Glu88 is likely to interact with the nicotinamide mononucleotide ribose of NAD+ in the ternary complex. This structure clearly explains the substrate specificity of IPMDH	Acidithiobacillus ferrooxidans

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Release 2023.1 (January 2023)