Literature summary for 4.2.1.33 extracted from

Yasutake, Y.; Yao, M.; Sakai, N.; Kirita, T.; Tanaka, I.
Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme (2004), J. Mol. Biol., 344, 325-333.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure isopropylmalate isomerase small subunit. Four molecules create an interlocked assembly with intermolecular disulfide linkages having a skewed 222 point-group symmetry. The structure reveals the formation of intermolecular disulfide linkages, and it provides insight into the dual substrate specificity of the enzyme	Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(2R,3S)-3-isopropylmalate	Pyrococcus horikoshii	the isopropylmalate isomerase small subunit of the hyperthermophilic archaea Pyrococcus horikoshii (PhIPMI-s) functions as isopropylmalate isomerase in the leucine biosynthesis pathway, and as homoaconitase (HACN) in the lysine biosynthesis pathway via alpha-aminoadipic acid	(2S)-2-isopropylmalate	-	?

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O59393	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(2R,3S)-3-isopropylmalate	the isopropylmalate isomerase small subunit of the hyperthermophilic archaea Pyrococcus horikoshii (PhIPMI-s) functions as isopropylmalate isomerase in the leucine biosynthesis pathway, and as homoaconitase (HACN) in the lysine biosynthesis pathway via alpha-aminoadipic acid	Pyrococcus horikoshii	(2S)-2-isopropylmalate	-	?

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Release 2023.1 (January 2023)