ENZYME entry: EC 1.14.14.38
Accepted Name |
Valine N-monooxygenase.
|
Alternative Name(s) |
CYP79D1. |
CYP79D2. |
Reaction catalysed |
L-valine + 2 O(2) + 2 [reduced NADPH--hemoprotein reductase] <=> (E)-2-methylpropanal oxime + 2 [oxidized NADPH--hemoprotein reductase] + CO(2) + 3 H(2)O |
Cofactor(s) |
Heme-thiolate.
|
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 1.14.13.117.
|
Cross-references |
BRENDA | 1.14.14.38 |
EC2PDB | 1.14.14.38 |
ExplorEnz | 1.14.14.38 |
PRIAM enzyme-specific profiles | 1.14.14.38 |
KEGG Ligand Database for Enzyme Nomenclature | 1.14.14.38 |
IUBMB Enzyme Nomenclature | 1.14.14.38 |
IntEnz | 1.14.14.38 |
MEDLINE | Find literature relating to 1.14.14.38 |
MetaCyc | 1.14.14.38 |
Rhea expert-curated reactions | 1.14.14.38 |
UniProtKB/Swiss-Prot |
|
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