Mechanistic implications and family relationships from the structure of dethiobiotin synthetase.
Alexeev, D., Baxter, R.L., Sawyer, L.(1994) Structure 2: 1061-1072
- PubMed: 7881906 
- DOI: https://doi.org/10.1016/s0969-2126(94)00109-x
- Primary Citation of Related Structures:  
1DBS - PubMed Abstract: 
Biotin is the vitamin essential for many biological carboxylation reactions, such as the conversion of acetyl-coenzyme A (CoA) to malonyl-CoA in fatty acid biosynthesis. Dethiobiotin synthetase (DTBS) facilitates the penultimate, ureido ring closure in biotin synthesis, which is a non-biotin-dependent carboxylation. DTBS displays no sequence similarity to any other protein in the database. Structural studies provide a molecular insight into the reaction mechanism of DTBS.
Organizational Affiliation: 
Edinburgh Centre for Molecular Recognition, Department of Biochemistry, University of Edinburgh, UK.