ENZYME entry: EC 1.14.14.39
Accepted Name |
Isoleucine N-monooxygenase.
|
Alternative Name(s) |
CYP79D3. |
CYP79D4. |
Reaction catalysed |
L-isoleucine + 2 O(2) + 2 [reduced NADPH--hemoprotein reductase] <=> (1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH--hemoprotein reductase] + CO(2) + 3 H(2)O |
Cofactor(s) |
Heme-thiolate.
|
Comment(s) |
- This enzyme, found in plants, catalyzes two successive
N-hydroxylations of L-isoleucine, the committed step in the
biosynthesis of the cyanogenic glucoside lotaustralin.
- The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine,
is labile and undergoes dehydration followed by decarboxylation,
producing the oxime.
- It is still not known whether the decarboxylation is spontaneous or
catalyzed by the enzyme.
- The enzyme can also accept L-valine, but with a lower activity.
- Cf. EC 1.14.14.38, valine N-monooxygenase.
- Formerly EC 1.4.13.117.
|
Cross-references |
BRENDA | 1.14.14.39 |
EC2PDB | 1.14.14.39 |
ExplorEnz | 1.14.14.39 |
PRIAM enzyme-specific profiles | 1.14.14.39 |
KEGG Ligand Database for Enzyme Nomenclature | 1.14.14.39 |
IUBMB Enzyme Nomenclature | 1.14.14.39 |
IntEnz | 1.14.14.39 |
MEDLINE | Find literature relating to 1.14.14.39 |
MetaCyc | 1.14.14.39 |
Rhea expert-curated reactions | 1.14.14.39 |
UniProtKB/Swiss-Prot |
|
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