Accepted name: 1,8-cineole 2-endo-monooxygenase
Reaction: 1,8-cineole + [reduced flavodoxin] + O2 = 2-endo-hydroxy-1,8-cineole + [oxidized flavodoxin] + H2O
Glossary: 1,8-cineole = 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane
2-endo-hydroxy-1,8-cineole = (1R,4S,6R)-1,3,3-trimethyl-2-oxabicyclo[2.2.2]octan-6-ol
Other name(s): P450cin; CYP176A; CYP176A1
Systematic name: 1,8-cineole,[reduced flavodoxin]:oxygen oxidoreductase (2-endo-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein that uses a flavodoxin-like redox partner to reduce the heme iron. Isolated from the bacterium Citrobacter braakii, which can use 1,8-cineole as the sole source of carbon.
1.  Hawkes, D.B., Adams, G.W., Burlingame, A.L., Ortiz de Montellano, P.R. and De Voss, J.J. Cytochrome P450cin (CYP176A), isolation, expression, and characterization. J. Biol. Chem. 277 (2002) 27725–27732. [PMID: 12016226]
2.  Meharenna, Y.T., Li, H., Hawkes, D.B., Pearson, A.G., De Voss, J. and Poulos, T.L. 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 (2004) 9487–9494. [PMID: 15260491]
3.  Kimmich, N., Das, A., Sevrioukova, I., Meharenna, Y., Sligar, S.G. and Poulos, T.L. Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin. J. Biol. Chem. 282 (2007) 27006–27011. [PMID: 17606612]
4.  Meharenna, Y.T., Slessor, K.E., Cavaignac, S.M., Poulos, T.L. and De Voss, J.J. The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin. J. Biol. Chem. 283 (2008) 10804–10812. [PMID: 18270198]
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