| EC |
1.14.14.99 |
| Accepted name: |
(S)-limonene 3-monooxygenase |
| Reaction: |
(S)-limonene + [reduced NADPH—hemoprotein reductase] + O2 = (–)-trans-isopiperitenol + [oxidized NADPH—hemoprotein reductase] + H2O |
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For diagram of perillyl alcohol, isopiperitol and carveol biosynthesis, click here |
| Glossary: |
limonene = a monoterpenoid
(S)-limonene = (–)-limonene |
| Other name(s): |
(–)-limonene 3-hydroxylase; (–)-limonene 3-monooxygenase; CYP71D15 (gene name) |
| Systematic name: |
(S)-limonene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating) |
| Comments: |
A cytochrome P-450 (heme-thiolate) protein from peppermint (Mentha piperita). |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 138066-92-9 |
| References: |
| 1. |
Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. 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 (1990) 219–226. [DOI] [PMID: 2297225] |
| 2. |
Lupien, S., Karp, F., Wildung, M. and Croteau, R. Regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha) species: cDNA isolation, characterization, and functional expression of (–)-4S-limonene-3-hydroxylase and (–)-4S-limonene-6-hydroxylase. Arch. Biochem. Biophys. 368 (1999) 181–192. [PMID: 10415126] |
| 3. |
Wust, M., Little, D.B., Schalk, M. and Croteau, R. Hydroxylation of limonene enantiomers and analogs by recombinant (–)-limonene 3- and 6-hydroxylases from mint (Mentha) species: evidence for catalysis within sterically constrained active sites. Arch. Biochem. Biophys. 387 (2001) 125–136. [PMID: 11368174] |
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| [EC 1.14.14.99 created 1992 as EC 1.14.13.47, modified 2003, transferred 2018 1.14.14.99] |
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