Issue 8, 2006

Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2′-deoxyadenosine substrates

Abstract

The fluorinase enzyme from Streptomyces cattleya displays an unusual ability in biocatalysis in that it forms a C–F bond. We now report that the enzyme will accept 2′-deoxyadenosine in place of adenosine substrates, and structural evidence reveals a reorganisation in hydrogen bonding to accommodate this substrate series. It emerges from this study that the enzyme does not require a planar ribose conformation of the substrate to catalyse C–F bond formation.

Graphical abstract: Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2′-deoxyadenosine substrates

Supplementary files

Article information

Article type
Communication
Submitted
13 Jan 2006
Accepted
22 Feb 2006
First published
08 Mar 2006

Org. Biomol. Chem., 2006,4, 1458-1460

Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2′-deoxyadenosine substrates

S. L. Cobb, H. Deng, A. R. McEwan, J. H. Naismith, D. O'Hagan and D. A. Robinson, Org. Biomol. Chem., 2006, 4, 1458 DOI: 10.1039/B600574H

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements