Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2′-deoxyadenosine substrates
- 1 January 2006
- journal article
- Published by Royal Society of Chemistry (RSC) in Organic & Biomolecular Chemistry
- Vol. 4 (8) , 1458-1460
- https://doi.org/10.1039/b600574h
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.Keywords
This publication has 17 references indexed in Scilit:
- Fluorinase mediated C–18F bond formation, an enzymatic tool for PET labellingChemical Communications, 2006
- The Fluorinase from Streptomyces cattleya Is Also a ChlorinaseAngewandte Chemie International Edition in English, 2006
- Insight into Enzymatic C−F Bond Formation from QM and QM/MM CalculationsJournal of the American Chemical Society, 2005
- Crystal structure and mechanism of a bacterial fluorinating enzymeNature, 2004
- Isolation and characterisation of 5′‐fluorodeoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleyaFEBS Letters, 2003
- Biosynthesis of an organofluorine moleculeNature, 2002
- Biosynthesis of fluorothreonine and fluoroacetic acid by the thienamycin producer, Streptomyces cattleya.The Journal of Antibiotics, 1986
- Convenient preparation of 5'-chloro-2',5'-dideoxyadenosineThe Journal of Organic Chemistry, 1979
- Improved synthesis of decarboxylated S-adenosylmethionine and related sulfonium compounds.CHEMICAL & PHARMACEUTICAL BULLETIN, 1978
- Nucleoside von fluor-zuckernCarbohydrate Research, 1970