Biotin synthase
From Wikipedia, the free encyclopedia
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 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.
Contents |
[edit] Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1R30.
[edit] References
- IUBMB entry for 2.8.1.6
- BRENDA references for 2.8.1.6 (Recommended.)
- PubMed references for 2.8.1.6
- PubMed Central references for 2.8.1.6
- Google Scholar references for 2.8.1.6
- Shiuan D, Campbell A (1988). "Transcriptional regulation and gene arrangement of Escherichia coli, Citrobacter freundii and Salmonella typhimurium biotin operons". Gene. 67: 203–11. doi: . 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: 29–35. doi: . PMID 8117110.
- Trainor DA, Parry RJ and Gitterman A (1980). "Biotin biosynthesis. 2. Stereochemistry of sulfur introduction at C-4 of dethiobiotin". J. Am. Chem. Soc. 102: 1467–1468. doi: .
- Lotierzo M, Tse Sum Bui B, Florentin D, Escalettes F, Marquet A (2005). "Biotin synthase mechanism: an overview". Biochem. Soc. Trans. 33: 820–3. doi: . 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: 76–9. doi: . 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: 8343–51. doi: . PMID 11444981.
[edit] External links
-
- The CAS registry number for this enzyme class is 80146-93-6.