ENZYME entry: EC 1.14.13.118

Accepted Name
Valine N-monooxygenase.
Reaction catalysed
L-valine + 2 H(+) + 2 NADPH + 2 O(2) <=> (Z)-2-methylpropanal oxime + CO(2) + 3 H(2)O + 2 NADP(+)
Cofactor(s)
Heme-thiolate.
Comment(s)
  • This enzyme catalyzes two successive N-hydroxylations of L-valine, the first committed steps in the biosynthesis of the cyanogenic glucoside linamarin in the plant Manihot esculenta (cassava).
  • The product of the two hydroxylations, N,N-dihydroxy-L-valine, is extremely labile and dehydrates spontaneously.
  • The dehydrated product is then subject to a decarboxylation that produces the oxime.
  • It is still not known whether the decarboxylation is spontaneous or catalyzed by the enzyme.
  • The product, (E)-2-methylpropanal oxime, undergoes a spontaneous isomerization to the (Z) form.
  • The enzyme can also accept L-isoleucine as substrate, with a lower activity.
  • It is different from EC 1.14.13.117 which prefers L-isoleucine.
Cross-references
BRENDA1.14.13.118
EC2PDB1.14.13.118
ExplorEnz1.14.13.118
PRIAM enzyme-specific profiles1.14.13.118
KEGG Ligand Database for Enzyme Nomenclature1.14.13.118
IUBMB Enzyme Nomenclature1.14.13.118
IntEnz1.14.13.118
MEDLINEFind literature relating to 1.14.13.118
MetaCyc1.14.13.118
UniProtKB/Swiss-Prot
Q9M7B8, C79D1_MANES;  Q9M7B7, C79D2_MANES;  

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