| Literature DB >> 16604208 |
Steven L Cobb1, Hai Deng, Andrew R McEwan, James H Naismith, David O'Hagan, David A Robinson.
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.Entities:
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Year: 2006 PMID: 16604208 PMCID: PMC3326537 DOI: 10.1039/b600574h
Source DB: PubMed Journal: Org Biomol Chem ISSN: 1477-0520 Impact factor: 3.876