1,8-Cineole 2-endo-monooxygenase
Identifiers
EC no.1.14.14.133
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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 2-endo-hydroxy-1,8-cineole + NADP+ + H2O

1,8-Cineole 2-endo-monooxygenase is a heme-thiolate protein (P-450).

References

  1. ^ Hawkes DB, Adams GW, Burlingame AL, Ortiz de Montellano PR, De Voss JJ (August 2002). "Cytochrome P450(cin) (CYP176A), isolation, expression, and characterization". The Journal of Biological Chemistry. 277 (31): 27725–32. doi:10.1074/jbc.M203382200. PMID 12016226.
  2. ^ Meharenna YT, Li H, Hawkes DB, Pearson AG, De Voss J, Poulos TL (July 2004). "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. doi:10.1021/bi049293p. PMID 15260491.
  3. ^ Kimmich N, Das A, Sevrioukova I, Meharenna Y, Sligar SG, Poulos TL (September 2007). "Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin". The Journal of Biological Chemistry. 282 (37): 27006–11. doi:10.1074/jbc.M703790200. PMID 17606612.
  4. ^ Meharenna YT, Slessor KE, Cavaignac SM, Poulos TL, De Voss JJ (April 2008). "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. doi:10.1074/jbc.M709722200. PMC 2447660. PMID 18270198.

External links

Cytochromes, oxygenases: cytochrome P450 (Most belong to EC 1.14)
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