1,8-Cineole 2-endo-monooxygenase

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
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 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.
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