PMID:9240449
| Citation |
Guianvarc'h, D, Florentin, D, Tse Sum Bui, B, Nunzi, F and Marquet, A (1997) Biotin synthase, a new member of the family of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical. Biochem. Biophys. Res. Commun. 236:402-6 |
|---|---|
| Abstract |
The fact that biotin synthase, from Escherichia coli and Bacillus sphaericus, requires S-adenosylmethionine and a reducing system led us to postulate that this synthase could belong to the family of enzymes which use S-adenosylmethionine as a source of deoxyadenosyl radical, namely pyruvate formate-lyase, lysine 2,3-aminomutase, and anaerobic ribonucleotide reductase. We describe here experiments with S-[2,8-(3)H] adenosylmethionine and S-adenosyl-[methyl-3H]methionine which allowed the identification and quantification of the expected cleavage products, deoxyadenosine, and methionine. They are formed in equimolar amounts, in a ratio close to 3 with respect to the biotin produced. We postulate a mechanism involving the homolytic cleavage of two C-H bonds which should consume two equivalents of S-adenosylmethionine. The observed excess of S-adenosylmethionine consumption is attributed to abortive processes. |
| Links | |
| Keywords |
Bacillus/enzymology; Biotin/biosynthesis; Escherichia coli/enzymology; Free Radicals; S-Adenosylmethionine/chemistry; S-Adenosylmethionine/metabolism; Sulfurtransferases/metabolism |
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