Biology:Isoleucine N-monooxygenase
| Isoleucine N-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.14.39 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Isoleucine N-monooxygenase (EC 1.14.14.39, CYP79D3, CYP79D4) is an enzyme with systematic name L-isoleucine,NADPH:oxygen oxidoreductase (N-hydroxylating).[1] It catalyses the following sequence of chemical reactions:
- REDIRECT Template:Chemical reaction
The enzyme uses molecular oxygen and reduced nicotinamide adenine dinucleotide phosphate (NADPH) to convert L-isoleucine first to its N-hydroxy derivative and then to N,N-dihydroxy-L-isoleucine. This compound is unstable and loses carbon dioxide and water to give the (1E,2S) isomer of 2-methylbutanal oxime.[2]
Isoleucine N-monooxygenase is a cytochrome P450 protein containing heme.[3] The product oxime is an intermediate in the biosynthesis of lotaustralin in Lotus japonicus.[2]
References
- ↑ "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". The Journal of Biological Chemistry 275 (3): 1966–75. January 2000. doi:10.1074/jbc.275.3.1966. PMID 10636899.
- ↑ 2.0 2.1 "Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus". Plant Physiology 135 (1): 71–84. May 2004. doi:10.1104/pp.103.038059. PMID 15122013.
- ↑ Enzyme 1.14.14.39 at KEGG Pathway Database.
External links
- Isoleucine+N-monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
