Biology:1,8-Cineole 2-endo-monooxygenase
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Short description: Class of enzymes
| 1,8-Cineole 2-endo-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.14.133 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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1,8-Cineole 2-endo-monooxygenase (EC 1.14.14.133, Formerly EC 1.14.13.156, P450cin, CYP176A, CYP176A1) is an enzyme with systematic name 1,8-cineole,NADPH:oxygen oxidoreductase (2-endo-hydroxylating).[1][2][3][4] This enzyme catalyses the following chemical reaction
- 1,8-cineole + NADPH + H+ + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2-endo-hydroxy-1,8-cineole + NADP+ + H2O
1,8-Cineole 2-endo-monooxygenase is a heme-thiolate protein (P-450).
References
- ↑ "Cytochrome P450(cin) (CYP176A), isolation, expression, and characterization". The Journal of Biological Chemistry 277 (31): 27725–32. August 2002. doi:10.1074/jbc.M203382200. PMID 12016226.
- ↑ "Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450cam". Biochemistry 43 (29): 9487–94. July 2004. doi:10.1021/bi049293p. PMID 15260491.
- ↑ "Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin". The Journal of Biological Chemistry 282 (37): 27006–11. September 2007. doi:10.1074/jbc.M703790200. PMID 17606612.
- ↑ "The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin". The Journal of Biological Chemistry 283 (16): 10804–12. April 2008. doi:10.1074/jbc.M709722200. PMID 18270198.
External links
- 1,8-cineole+2-endo-monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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