2.8.1.6	dethiobiotin + sulfur	hypothesis: sulfur of biotin is derived from the [Fe-S] center of the enzyme	
2.8.1.6	dethiobiotin + sulfur	catalyzes the last step of the biosynthesis of biotin	
2.8.1.6	dethiobiotin + sulfur	expression of the BIO2 gene appears to be induced under biotin-limiting conditions	
2.8.1.6	dethiobiotin + sulfur	biotin synthase is active for only one turnover, during which the [2Fe-2S]2+ cluster is destroyed, one sulfide from the cluster is incorporated as the biotin thiophane sulfur, while Fe2+ ions and the remaining S2- ion are released from the protein	
2.8.1.6	dethiobiotin + sulfur + 2 S-adenosyl-L-methionine	9-mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase	
2.8.1.6	dethiobiotin + sulfur + 2 S-adenosyl-L-methionine	The biotin synthase (BioB) reaction does not require pyridoxal phosphate in vivo. Therefore, the biotin sulfur atom cannot be derived via an intrinsic pyridoxal phosphate-dependent BioB cysteine desulfurase activity	
2.8.1.6	dethiobiotin + sulfur + S-adenosyl-L-methionine	-	
2.8.1.6	dethiobiotin + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] ferredoxin	-	
2.8.1.6	additional information	rate-limiting enzyme for biotin synthesis