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Your query returned 1 entry. Printable version
EC | 1.14.14.39 | ||||
Accepted name: | isoleucine N-monooxygenase | ||||
Reaction: | L-isoleucine + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction) (1a) L-isoleucine + [reduced NADPH—hemoprotein reductase] + O2 = N-hydroxy-L-isoleucine + [oxidized NADPH—hemoprotein reductase] + H2O (1b) N-hydroxy-L-isoleucine + [reduced NADPH—hemoprotein reductase] + O2 = N,N-dihydroxy-L-isoleucine + [oxidized NADPH—hemoprotein reductase] + H2O (1c) N,N-dihydroxy-L-isoleucine = (1E,2S)-2-methylbutanal oxime + CO2 + H2O (spontaneous) |
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Other name(s): | CYP79D3 (gene name); CYP79D4 (gene name) | ||||
Systematic name: | L-isoleucine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating) | ||||
Comments: | This cytochrome P-450 (heme-thiolate) enzyme, found in plants, catalyses two successive N-hydroxylations of L-isoleucine, the committed step in the biosynthesis of the cyanogenic glucoside lotaustralin. The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine, is labile and undergoes dehydration followed by decarboxylation, producing the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-valine, but with a lower activity. cf. EC 1.14.14.38, valine N-monooxygenase. | ||||
Links to other databases: | BRENDA, EXPASY, Gene, KEGG, MetaCyc | ||||
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