Biology:1,8-Cineole 2-endo-monooxygenase

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Short description: Class of enzymes
1,8-Cineole 2-endo-monooxygenase
Identifiers
EC number1.14.14.133
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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

  1. ↑ "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. 
  2. ↑ "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. 
  3. ↑ "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. 
  4. ↑ "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



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