Fluorinase

Fluorinase is an enzyme that catalyzes the chemical reaction of a fluoride ion with S-adenosyl-L-methionine to produce 5'-fluoro-5'-deoxyadenosine and L-methionine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group transferases. The systematic name of this enzyme class is fluoride:5'-deoxyadenosine 5'-fluorotransferase. Other names in common use include 5'-fluoro-5'-deoxyadenosine synthase, and SAM:fluoride adenosyltransferase.

Function

Fluorinase is a key enzyme in the biosynthesis of fluorometabolites. It is the only known enzyme capable of forming a carbon-fluorine bond, a key step in the biosynthesis of fluoroacetate and 4-fluorothreonine in certain species of Streptomyces. The enzyme is unique in that it uses a fluoride ion as a substrate, whereas most other enzymes use a cofactor or a metal ion.

Structure

Fluorinase is a monomeric protein with a molecular weight of approximately 30 kDa. The enzyme has a unique active site that is capable of binding both the fluoride ion and S-adenosyl-L-methionine. The active site is composed of a cysteine residue, which is thought to be involved in the formation of the carbon-fluorine bond, and a histidine residue, which is thought to be involved in the deprotonation of the fluoride ion.

Biological Significance

The ability of fluorinase to form a carbon-fluorine bond is of significant interest in the field of biochemistry. The carbon-fluorine bond is one of the strongest in organic chemistry, and its formation by an enzyme is a rare and remarkable event. The study of fluorinase and its mechanism of action can provide insights into the nature of enzymatic catalysis and the evolution of enzyme function.

See Also

• Fluorometabolite
• Streptomyces
• Enzyme

References

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