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Information on EC 1.14.14.38 - valine N-monooxygenase

for references in articles please use BRENDA:EC1.14.14.38
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IUBMB 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.
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The enzyme appears in viruses and cellular organisms
Synonyms
n-hydroxylating cytochrome p450, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = (E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
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overall reaction
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L-valine + [reduced NADPH-hemoprotein reductase] + O2 = N-hydroxy-L-valine + [oxidized NADPH-hemoprotein reductase] + H2O
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(1a)
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N,N-dihydroxy-L-valine = (E)-2-methylpropanal oxime + CO2 + H2O
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spontaneous
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N-hydroxy-L-valine + [reduced NADPH-hemoprotein reductase] + O2 = N,N-dihydroxy-L-valine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(1b)
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