(S)-limonene 7-monooxygenase
| (S)-limonene 7-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.14.52 | ||||||||
| CAS no. | 122653-75-2 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
(S)-limonene 7-monooxygenase (EC 1.14.14.52) is an enzyme that catalyzes the chemical reaction
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-Perillyl_alcohol.svg.png)
The four substrates of this enzyme are (−)-(S)-limonene, reduced nicotinamide adenine dinucleotide phosphate (NADPH), oxygen, and a proton. Its products are (−)-perillyl alcohol, oxidised NADP+, and water.[1][2]
This enzyme is a cytochrome P450 protein containing heme. This oxidoreductase, which uses molecular oxygen as oxidant is in a group with systematic name (S)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating). Other names in common use include (−)-limonene 7-monooxygenase, (−)-limonene hydroxylase, (−)-limonene monooxygenase, and (−)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating).[1] In Perilla frutescens it is part of the biosynthetic pathway to perillaldehyde.[2]
References
- 1 2 Enzyme 1.14.14.52 at KEGG Pathway Database.
- 1 2 Karp F, Mihaliak CA, Harris JL, Croteau R (1990). "Monoterpene biosynthesis: specificity of the hydroxylations of (−)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves". Arch. Biochem. Biophys. 276 (1): 219–26. doi:10.1016/0003-9861(90)90029-X. PMID 2297225.