EC 1.14.14.133 - 1,8-cineole 2-endo-monooxygenase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.14.14.133

Names

Accepted name:
1,8-cineole 2-endo-monooxygenase
Other names:
P450cin
CYP176A
CYP176A1
Systematic name:
1,8-cineole,[reduced flavodoxin]:oxygen oxidoreductase (2-endo-hydroxylating)

Reaction

Cofactor

Comments:

A cytochrome P450 (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. Formerly EC 1.14.13.156.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Hawkes, D. B., Adams, G. W., Burlingame, A. L., Ortiz de Montellano, P. R., De Voss, J. J.
    Cytochrome P450(cin) (CYP176A), isolation, expression, and characterization.
    J. Biol. Chem. 277 : 27725-27732 (2002). [PMID: 12016226]
  2. Meharenna, Y. T., Li, H., Hawkes, D. B., Pearson, A. G., De Voss, J., 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 : 9487-9494 (2004). [PMID: 15260491]
  3. Kimmich, N., Das, A., Sevrioukova, I., Meharenna, Y., Sligar, S. G., Poulos, T. L.
    Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin.
    J. Biol. Chem. 282 : 27006-27011 (2007). [PMID: 17606612]
  4. Meharenna, Y. T., Slessor, K. E., Cavaignac, S. M., Poulos, T. L., De Voss, J. J.
    The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin.
    J. Biol. Chem. 283 : 10804-10812 (2008). [PMID: 18270198]

[EC 1.14.14.133 created 2012 as EC 1.14.13.156, transferred 2018 to EC 1.14.14.133]