PMID:15911379

Citation	Choi-Rhee, E and Cronan, JE (2005) A nucleosidase required for in vivo function of the S-adenosyl-L-methionine radical enzyme, biotin synthase. Chem. Biol. 12:589-93
Abstract	Biotin synthase is an S-adenosyl-L-methionine (SAM) radical enzyme that inserts sulfur into dethiobiotin to produce biotin. The reaction proceeds through 5'-deoxyadenosyl radical intermediates that become reduced during the sulfur insertion step to give another product of the reaction, 5'-deoxyadenosine. We report that Escherichia coli strains lacking the 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase encoded by the pfs gene are deficient in biotin synthase activity due to accumulation of 5'-deoxyadenosine, a new substrate of the pfs-encoded nucleosidase. Physiological experiments indicate that lipoic acid synthase, another SAM radical enzyme, is also inhibited by 5'-deoxyadenosine accumulation.
Links	PubMed Online version:10.1016/j.chembiol.2005.04.012
Keywords	Biotin/analogs & derivatives; Biotin/pharmacology; Deoxyadenosines/pharmacology; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins/antagonists & inhibitors; Escherichia coli Proteins/metabolism; Mutation; N-Glycosyl Hydrolases/genetics; N-Glycosyl Hydrolases/metabolism; Sulfurtransferases/antagonists & inhibitors; Sulfurtransferases/metabolism
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