EC Number   |
Natural Substrates |
|---|
    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 | more |
rate-limiting enzyme for biotin synthesis |
