IUBMB Enzyme Nomenclature

EC 1.14.13.156

Accepted name: 1,8-cineole 2-endo-monooxygenase

Reaction: 1,8-cineole + NADPH + H+ + O2 = 2-endo-hydroxy-1,8-cineole + NADP+ + H2O

For diagram of reaction click here.

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,NADPH:oxygen oxidoreductase (2-endo-hydroxylating)

Comments: A heme-thiolate protein (P-450) which 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.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

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]

[EC 1.14.13.156 created 2012]


Return to EC 1.14.13 home page
Return to EC 1.14 home page
Return to EC 1 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page