Biotin synthase

In enzymology, a biotin synthase (EC 2.8.1.6) is an enzyme that catalyzes the chemical reaction

dethiobiotin + sulfur + 2 S-adenosyl-L-methionine biotin + 2 L-methionine + 2 5'-deoxyadenosine

The 3 substrates of this enzyme are dethiobiotin, sulfur, and S-adenosyl-L-methionine, whereas its 3 products are biotin, L-methionine, and 5'-deoxyadenosine.

This radical SAM enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is dethiobiotin:sulfur sulfurtransferase. This enzyme participates in biotin metabolism. It employs one cofactor, iron-sulfur.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1R30.

References

• Shiuan D, Campbell A (1988). "Transcriptional regulation and gene arrangement of Escherichia coli, Citrobacter freundii and Salmonella typhimurium biotin operons". Gene. 67 (2): 203–11. doi:10.1016/0378-1119(88)90397-6. PMID 2971595. 
• Zhang S, Sanyal I, Bulboaca GH, Rich A, Flint DH (1994). "The gene for biotin synthase from Saccharomyces cerevisiae: cloning, sequencing, and complementation of Escherichia coli strains lacking biotin synthase". Arch. Biochem. Biophys. 309 (1): 29–35. doi:10.1006/abbi.1994.1079. PMID 8117110. 
• Trainor DA, Parry RJ, Gitterman A (1980). "Biotin biosynthesis. 2. Stereochemistry of sulfur introduction at C-4 of dethiobiotin". J. Am. Chem. Soc. 102 (4): 1467–1468. doi:10.1021/ja00524a064. 
• Lotierzo M, Tse Sum Bui B, Florentin D, Escalettes F, Marquet A (2005). "Biotin synthase mechanism: an overview". Biochem. Soc. Trans. 33 (Pt 4): 820–3. doi:10.1042/BST0330820. PMID 16042606. 
• Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL (2004). "Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme". Science. 303 (5654): 76–9. doi:10.1126/science.1088493. PMC 1456065. PMID 14704425. 
• Ugulava NB, Gibney BR, Jarrett JT (2001). "Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions". Biochemistry. 40 (28): 8343–51. doi:10.1021/bi0104625. PMC 1538964. PMID 11444981.