The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

bioD  -  dithiobiotin synthetase

Escherichia coli O157:H7 str. Sakai

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of bioD


Psychiatry related information on bioD


High impact information on bioD


Associations of bioD with chemical compounds


Analytical, diagnostic and therapeutic context of bioD

  • Sequence analysis of this fragment revealed that it is closely related to a family of ATP-dependent enzymes that also includes dethiobiotin synthetase and the synthetase domains of two amidotransferases involved in cobalamin biosynthesis, cobyrinic acid a,c-diamide synthase (CobB) and cobyric acid synthase (CobQ) [8].


  1. Snapshot of a phosphorylated substrate intermediate by kinetic crystallography. Käck, H., Gibson, K.J., Lindqvist, Y., Schneider, G. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  2. Mechanistic implications and family relationships from the structure of dethiobiotin synthetase. Alexeev, D., Baxter, R.L., Sawyer, L. Structure (1994) [Pubmed]
  3. Sequence and crystallization of Escherichia coli dethiobiotin synthetase, the penultimate enzyme of biotin biosynthesis. Alexeev, D., Bury, S.M., Boys, C.W., Turner, M.A., Sawyer, L., Ramsey, A.J., Baxter, H.C., Baxter, R.L. J. Mol. Biol. (1994) [Pubmed]
  4. Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets. Endrizzi, J.A., Kim, H., Anderson, P.M., Baldwin, E.P. Biochemistry (2004) [Pubmed]
  5. Active site mutants of Escherichia coli dethiobiotin synthetase: effects of mutations on enzyme catalytic and structural properties. Yang, G., Sandalova, T., Lohman, K., Lindqvist, Y., Rendina, A.R. Biochemistry (1997) [Pubmed]
  6. Mode of action of the biotin antimetabolites actithiazic acid and alpha-methyldethiobiotin. Eisenberg, M.A., Hsiung, S.C. Antimicrob. Agents Chemother. (1982) [Pubmed]
  7. In vitro synthesis and and regulation of the biotin enzymes of Escherichia coli K-12. Prakash, O., Eisenberg, M.A. J. Bacteriol. (1978) [Pubmed]
  8. The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase. Galperin, M.Y., Grishin, N.V. Proteins (2000) [Pubmed]
WikiGenes - Universities