1,8-Cineole 2-endo-monooxygenase

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1,8-Cineole 2-endo-monooxygenase
Identifiers
EC number 1.14.13.156
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

1,8-Cineole 2-endo-monooxygenase (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[edit]

  1. ^ Hawkes, D.B.; Adams, G.W.; Burlingame, A.L.; Ortiz de Montellano, P.R.; De Voss, J.J. (2002). "Cytochrome P450cin (CYP176A), isolation, expression, and characterization". J. Biol. Chem. 277 (31): 27725–27732. doi:10.1074/jbc.M203382200. PMID 12016226. 
  2. ^ Meharenna, Y.T.; Li, H.; Hawkes, D.B.; Pearson, A.G.; De Voss, J.; Poulos, T.L. (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): 9487–9494. doi:10.1021/bi049293p. PMID 15260491. 
  3. ^ Kimmich, N.; Das, A.; Sevrioukova, I.; Meharenna, Y.; Sligar, S.G.; Poulos, T.L. (2007). "Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin". J. Biol. Chem. 282 (37): 27006–27011. doi:10.1074/jbc.M703790200. PMID 17606612. 
  4. ^ Meharenna, Y.T.; Slessor, K.E.; Cavaignac, S.M.; Poulos, T.L.; De Voss, J.J. (2008). "The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin". J. Biol. Chem. 283 (16): 10804–10812. doi:10.1074/jbc.M709722200. PMC 2447660Freely accessible. PMID 18270198. 

External links[edit]