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Your query returned 1 entry. 
Printable version
| EC | 1.14.14.38 | ||||
| Accepted name: | valine N-monooxygenase | ||||
| Reaction: | L-valine + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (E)-2-methylpropanal oxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction) (1a) L-valine + [reduced NADPH—hemoprotein reductase] + O2 = N-hydroxy-L-valine + [oxidized NADPH—hemoprotein reductase] + H2O (1b) N-hydroxy-L-valine + [reduced NADPH—hemoprotein reductase] + O2 = N,N-dihydroxy-L-valine + [oxidized NADPH—hemoprotein reductase] + H2O (1c) N,N-dihydroxy-L-valine = (E)-2-methylpropanal oxime + CO2 + H2O |
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| Other name(s): | CYP79D1; CYP79D2 | ||||
| Systematic name: | L-valine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating) | ||||
| Comments: | A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses two successive N-hydroxylations of L-valine, the committed step in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava). The product of the two hydroxylations, N,N-dihydroxy-L-valine, is labile and undergoes dehydration and decarboxylation that produce the (E) isomer of the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-isoleucine as substrate, with a lower activity. It is different from EC 1.14.14.39, isoleucine N-monooxygenase, which prefers L-isoleucine. | ||||
| Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||
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