Valine N-monooxygenase
| Valine N-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.13.118 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Valine N-monooxygenase (EC 1.14.13.118, CYP79D1, CYP79D2) is an enzyme with systematic name L-valine,NADPH:oxygen oxidoreductase (N-hydroxylating).[1][2] This enzyme catalyses the following chemical reaction
- L-valine + 2 O2 + 2 NADPH + 2 H+ (E)-2-methylpropanal oxime + 2 NADP+ + CO2 + 3 H2O (overall reaction)
- (1a) L-valine + O2 + NADPH + H+ N-hydroxy-L-valine + NADP+ + H2O
- (1b) N-hydroxy-L-valine + O2 + NADPH + H+ N,N-dihydroxy-L-valine + NADP+ + H2O
- (1c) N,N-dihydroxy-L-valine (E)-2-methylpropanal oxime + CO2 + H2O (spontaneous reaction)
Valine N-monooxygenase is a heme-thiolate protein (P-450).
References
- ↑ Andersen, M.D.; Busk, P.K.; Svendsen, I.; Moller, B.L. (2000). "Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes". J. Biol. Chem. 275 (3): 1966–1975. doi:10.1074/jbc.275.3.1966. PMID 10636899.
- ↑ Forslund, K.; Morant, M.; Jorgensen, B.; Olsen, C.E.; Asamizu, E.; Sato, S.; Tabata, S.; Bak, S. (2004). "Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus". Plant Physiol. 135 (1): 71–84. doi:10.1104/pp.103.038059. PMC 429334
. PMID 15122013.
External links
- Valine N-monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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