The fluorinase, the chlorinase and the duf-62 enzymes

Hai Deng, David O’Hagan

Research output: Contribution to journalArticlepeer-review

59 Citations (Scopus)


The fluorinase from Streptomyces cattleya and chlorinase from Salinispora tropica have a commonality in that they mediate nucleophilic reactions of their respective halide ions to the C-5' carbon of S-adenosyl-l-methionine (SAM). These enzyme reactions fall into the relatively small group of SN2 substitution reactions found in enzymology. These enzymes have some homology to a larger class of proteins expressed by the duf-62 gene, of which around 200 representatives have been sequenced and deposited in databases. The duf-62 genes express a protein which mediates a hydrolytic cleavage of SAM to generate adenosine and l-methionine. Superficially this enzyme operates very similarly to the halogenases in that water/hydroxide replaces the halide ion. However structural examination of the duf-62 gene product reveals a very different organisation of the active site suggesting a novel mechanism for water activation.
Original languageEnglish
Pages (from-to)582-592
Number of pages10
JournalCurrent Opinion in Chemical Biology
Issue number5
Early online date31 Jul 2008
Publication statusPublished - Oct 2008


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