(+)-Menthofuran synthase
(Redirected from Menthofuran synthase)
| (+)-Menthofuran synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.14.143 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
(+)-Menthofuran synthase (EC 1.14.14.143, menthofuran synthase, (+)-pulegone 9-hydroxylase, (+)-MFS, cytochrome P450 menthofuran synthase) is an enzyme with systematic name (+)-pulegone,NADPH:oxygen oxidoreductase (9-hydroxylating).[1] This enzyme catalyses the following chemical reaction
-pulegone.svg)
-menthofuran.svg)
The enzyme is a cytochrome P450 protein containing heme, isolated from peppermint. It requires a partner cytochrome P450 reductase for functional expression. This uses nicotinamide adenine dinucleotide phosphate.[2][3]
References
[edit]- ↑ Bertea CM, Schalk M, Karp F, Maffei M, Croteau R (June 2001). "Demonstration that menthofuran synthase of mint (Mentha) is a cytochrome P450 monooxygenase: cloning, functional expression, and characterization of the responsible gene". Archives of Biochemistry and Biophysics. 390 (2): 279–86. doi:10.1006/abbi.2001.2378. PMID 11396930.
- ↑ Enzyme 1.14.14.143 at KEGG Pathway Database.
- ↑ Mahmoud SS, Croteau RB (November 2003). "Menthofuran regulates essential oil biosynthesis in peppermint by controlling a downstream monoterpene reductase". Proceedings of the National Academy of Sciences of the United States of America. 100 (24): 14481–6. Bibcode:2003PNAS..10014481M. doi:10.1073/pnas.2436325100. PMC 283617. PMID 14623962.
External links
[edit]- (+)-menthofuran+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
