3-Isopropylmalate dehydratase (E.C.4.2.1.33) is an aconitase homologue,[1][2][3] which catalyses the isomerisation of 2-isopropylmalate to 3-isopropylmalate, via dehydration, in the biosynthesis of leucine.
References
^Gross SR, Burns RO, Umbarger HE (1963). "The biosynthesis of leucine. II. The enzymic isomerization of beta-carboxy-beta-hydroxyisocaproate and alpha-hydroxy-beta-carboxyisocaproate". Biochemistry. 2 (5): 1046–52. doi:10.1021/bi00905a023. PMID14087357.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^Calvo JM, Stevens CM, Kalyanpur MG, Umbarger HE (December 1964). "The absolute configuration of alpha-hydroxy-beta-carboxyisocaproic acid (3-isopropylmalic acid), an intermediate in leucine biosynthesis". Biochemistry. 3 (12): 2024–7. doi:10.1021/bi00900a043. PMID14269331.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^Cole FE, Kalyanpur MG, Stevens CM (August 1973). "Absolute configuration of alpha isopropylmalate and the mechanism of its conversion to beta isopropylmalate in the biosynthesis of leucine". Biochemistry. 12 (17): 3346–50. doi:10.1021/bi00741a031. PMID4270046.{{cite journal}}: CS1 maint: multiple names: authors list (link)
