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

Org Biomol Chem. 2006 Apr 21;4(8):1458-60. doi: 10.1039/b600574h. Epub 2006 Mar 8.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Binding Sites
  • Chlorides / chemistry
  • Crystallography, X-Ray
  • Deoxyadenosines / chemistry*
  • Fluorides / chemistry
  • Hydrogen Bonding
  • Models, Molecular
  • Molecular Structure
  • Oxidoreductases / chemistry*
  • Streptomyces / classification
  • Streptomyces / enzymology*
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Chlorides
  • Deoxyadenosines
  • Oxidoreductases
  • fluorinase
  • 2'-deoxyadenosine
  • Fluorides