Adenosyl-fluoride synthase
Adenosyl-fluoride synthase | |||||||||
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Identifiers | |||||||||
EC number | 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 | ||||||||
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In enzymology, an adenosyl-fluoride synthase (EC 2.5.1.63) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + fluoride 5'-deoxy-5'-fluoroadenosine + L-methionine
Thus, the two substrates of this enzyme are S-adenosyl-L-methionine and fluoride, whereas its two products are 5'deoxy-5'-fluoroadenosine and L-methionine.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is S-adenosyl-L-methionine:fluoride adenosyltransferase. This enzyme is also called fluorinase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1RQP, 1RQR, 2C2W, 2C4T, 2C4U, 2C5B, 2C5H, 2CBX, and 2CC2.
See also
- Carbon–fluorine bond
- Organofluorine
References
- O'Hagan D, Schaffrath C, Cobb SL, Hamilton JT, Murphy CD (2002). "Biochemistry: biosynthesis of an organofluorine molecule". Nature. 416 (6878): 279. doi:10.1038/416279a. PMID 11907567.
- Naismith JH; Huang, F; Deng, H; Schaffrath, C; Spencer, JB; O'Hagan, D; Naismith, JH (2004). "Crystal structure and mechanism of a bacterial fluorinating enzyme". Nature. 427 (6974): 561–5. doi:10.1038/nature02280. PMID 14765200.