Fluorinase
| Fluorinase (adenosyl-fluoride synthase) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.63 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
The fluorinase enzyme (EC 2.5.1.63, also known as adenosyl-fluoride synthase) catalyzes the reaction between fluoride ion and the co-factor S-adenosyl-L-methionine to generate L-methionine and 5'-fluoro-5'-deoxyadenosine, the first committed product of the fluorometabolite biosynthesis pathway. The fluorinase was originally isolated from the soil bacterium Streptomyces cattleya, but homologues have since been identified in a number of other bacterial species, including Streptomyces sp. MA37, Nocardia brasiliensis and Actinoplanes sp. N902-109. This is the only known enzyme capable of catalysing the formation of a carbon-fluorine bond, the strongest single bond in organic chemistry.
A homologous chlorinase enzyme, which catalyses the same reaction with chloride rather than fluoride ion, has been isolated from Salinospora tropica, from the biosynthetic pathway of salinosporamide A.