Biotin Synthase, a New Member of the Family of Enzymes Which Uses S-Adenosylmethionine as a Source of Deoxyadenosyl Radical

The fact that biotin synthase, fromEscherichia coliandBacillus sphaericus,requiresS-adenosylmethionine and a reducing system led us to postulate that this synthase could belong to the family of enzymes which useS-adenosylmethionine as a source of deoxyadenosyl radical, namely pyruvate formate-lyase,...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-07, Vol.236 (2), p.402-406
Main Authors: Guianvarc'h, Dominique, Florentin, Dominique, Bui, Bernadette Tse Sum, Nunzi, Frederic, Marquet, Andrée
Format: Article
Language:English
Subjects:
Bacillus - enzymology
Biotin - biosynthesis
Escherichia coli - enzymology
Free Radicals
S-Adenosylmethionine - chemistry
S-Adenosylmethionine - metabolism
Sulfurtransferases - metabolism
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Summary:The fact that biotin synthase, fromEscherichia coliandBacillus sphaericus,requiresS-adenosylmethionine and a reducing system led us to postulate that this synthase could belong to the family of enzymes which useS-adenosylmethionine as a source of deoxyadenosyl radical, namely pyruvate formate-lyase, lysine 2,3-aminomutase, and anaerobic ribonucleotide reductase. We describe here experiments withS-[2,8-3H] adenosylmethionine andS-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 ofS-adenosylmethionine. The observed excess ofS-adenosylmethionine consumption is attributed to abortive processes.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.6952