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 |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.14.14.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-