Campus Units

Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of

Document Type

Article

Publication Version

Accepted Manuscript

Publication Date

9-28-2017

Journal or Book Title

Organic & Biomolecular Chemistry

Volume

15

Issue

36

First Page

7566

Last Page

7571

DOI

10.1039/C7OB01819C

Abstract

Bacteria can produce gibberellin plant hormones. While the bacterial biosynthetic pathway is similar to that of plants, the individual enzymes are very distantly related and arose via convergent evolution. The cytochromes P450 (CYPs) that catalyze the multi-step oxidation of the alkane precursor ent-kaurene (1) to ent-kauren-19-oic acid (5), are called ent-kaurene oxidase (KO), and in plants are from the CYP701 family, and share less than 19% amino acid sequence identity with those from bacteria, which are from the phylogenetically distinct CYP117 family. Here the reaction series catalyzed by CYP117 was examined by 18O2 labeling experiments, the results indicate successive hydroxylation of 1 to ent-kauren-19-ol (2) and then ent-kauren-19,19-diol (3) and most likely an intervening dehydration to ent-kauren-19-al (4) prior to the concluding hydroxylation to 5. Accordingly, the bacterial and plant KOs converged on catalysis of the same series of reactions, despite their independent evolutionary origin.

Comments

This is a manuscript of an article published as Nagel, Raimund, and Reuben J. Peters. "18 O 2 labeling experiments illuminate the oxidation of ent-kaurene in bacterial gibberellin biosynthesis." Organic & biomolecular chemistry 15, no. 36 (2017): 7566-7571. doi: 10.1039/C7OB01819C. Posted with permission.

Copyright Owner

The Royal Society of Chemistry

Language

en

File Format

application/pdf

Published Version

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