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ENZYME

ENZYME entry: EC 1.14.14.38

PURL: https://purl.expasy.org/enzyme/EC/1.14.14.38
Accepted Name
valine N-monooxygenase
Alternative Name(s)
CYP79D1
CYP79D2
Reaction catalysed
L-valine + 2 reduced [NADPH--hemoprotein reductase] + 2 O2 = (E)-2-methylpropanal oxime + 2 oxidized [NADPH--hemoprotein reductase] + CO2 + 3 H2O + 2 H(+)
Comment(s)
  • This enzyme catalyzes 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 catalyzed 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.
  • Formerly EC 1.14.13.118.
Cross-references
BRENDA1.14.14.38
EC2PDB1.14.14.38
ExplorEnz1.14.14.38
KEGG Ligand Database for Enzyme Nomenclature1.14.14.38
IUBMB Enzyme Nomenclature1.14.14.38
MEDLINEFind literature relating to 1.14.14.38
MetaCyc1.14.14.38
Rhea expert-curated reactions1.14.14.38
UniProtKB/Swiss-Prot
Q9M7B8, C79D1_MANESQ9M7B7, C79D2_MANESQ6J541, C79D3_LOTJA
Q6J540, C79D4_LOTJA

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