1,8-Cineole 2-endo-monooxygenase

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
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ 2-endo-hydroxy-1,8-cineole + NADP⁺ + H₂O

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

References

1. Hawkes, D.B., Adams, G.W., Burlingame, A.L., Ortiz de Montellano, P.R. and De Voss, J.J. (2002). "Cytochrome P450_cin (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. and Poulos, T.L. (2004). "Crystal structure of P450_cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450_cam". Biochemistry 43 (29): 9487–9494. doi:10.1021/bi049293p. PMID 15260491.
3. Kimmich, N., Das, A., Sevrioukova, I., Meharenna, Y., Sligar, S.G. and Poulos, T.L. (2007). "Electron transfer between cytochrome P450_cin 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. and 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 2447660. PMID 18270198.

External links

• 1,8-cineole 2-endo-monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)