Moonlighting cytochrome P450 monooxygenases

23Citations
Citations of this article
45Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

Recently, cytochrome P450 170A1 (CYP170A1) has been found to be a bifunctional protein, which catalyzes both monooxygenase activity and terpene synthase activity by two distinct active sites in the well-established P450 protein structure. Therefore, CYP170A1 is identified clearly as a moonlighting protein. The known activities of a small number of the 13,000 members of the P450 superfamily fall into two general classes: promiscuous enzymes that are not considered as moonlighting and forms that participate in biosynthesis of endogenous compounds, such as steroids, vitamins and play different roles in different tissues, sometimes being moonlighting enzymes. Here, we review examples of moonlighting P450, which add to our understanding of the large CYP superfamily. © 2011 IUBMB.

Cite

CITATION STYLE

APA

Zhao, B., & Waterman, M. R. (2011, July). Moonlighting cytochrome P450 monooxygenases. IUBMB Life. https://doi.org/10.1002/iub.501

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free