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


High impact information on bioD

  • The existence of the second postulated intermediate, a mixed carbamic-phosphoric anhydride formed when the carbamate is phosphorylated by ATP, is consistent with the cleavage of the gamma-phosphoryl group of ATP seen in DTBS reaction mixtures [Baxter, R. L., & Baxter, H. C. (1994) J. Chem. Soc., Chem. Commun., 759-760] [2].
  • Dethiobiotin synthetase (DTBS) catalyzes the formation of the cyclic urea, dethiobiotin (DTB), from (7R,8S)-diaminononanoic acid (DAPA), CO2, and ATP; the other products of the reaction are ADP and Pi [2].
  • Five active site residues, Thr11, Glu12, Lys15, Lys37, and Ser41, implicated by the protein crystal structure studies of Escherichia coli DTBS, were mutated to determine their function in catalysis and substrate binding [3].
  • Replacement of Thr11 with valine resulted in a 24,000-fold increase in the Km(ATP) with little or no change in the Kd(ATP), KM(DAPA) and DTBS k(cat), suggesting an essential role for this residue in the steady-state affinity for ATP [3].
  • (3) The N7-DAPA-carbamate mimic, 3-(1-aminoethyl)nonanedioic acid, in which the carbamate nitrogen was replaced with a methylene group, cyclized to the corresponding lactam in the presence of DTBS and ATP; ADP and P(i) were also formed.(ABSTRACT TRUNCATED AT 250 WORDS)[4]

Biological context of bioD


Associations of bioD with chemical compounds


Analytical, diagnostic and therapeutic context of bioD

  • Second, a moderately stable intermediate that could be labeled with either 14CO2, [gamma-33P]ATP, [9-3H]DAPA, or [1,7-14C]DAPA was trapped by quenching DTBS reactions at pH 4 and isolated by thin-layer chromatography [2].


  1. Genomic organization of the biotin biosynthetic genes of coryneform bacteria: cloning and sequencing of the bioA-bioD genes from Brevibacterium flavum. Hatakeyama, K., Hohama, K., Vertès, A.A., Kobayashi, M., Kurusu, Y., Yukawa, H. DNA Seq. (1993) [Pubmed]
  2. Isolation and chemistry of the mixed anhydride intermediate in the reaction catalyzed by dethiobiotin synthetase. Gibson, K.J. Biochemistry (1997) [Pubmed]
  3. 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]
  4. Dethiobiotin synthetase: the carbonylation of 7,8-diaminonanoic acid proceeds regiospecifically via the N7-carbamate. Gibson, K.J., Lorimer, G.H., Rendina, A.R., Taylor, W.S., Cohen, G., Gatenby, A.A., Payne, W.G., Roe, D.C., Lockett, B.A., Nudelman, A. Biochemistry (1995) [Pubmed]
  5. Complete sequence and organization of the Serratia marcescens biotin operon. Sakurai, N., Akatsuka, H., Kawai, E., Imai, Y., Komatsubara, S. Microbiology (Reading, Engl.) (1996) [Pubmed]
  6. Mechanistic implications and family relationships from the structure of dethiobiotin synthetase. Alexeev, D., Baxter, R.L., Sawyer, L. Structure (1994) [Pubmed]
  7. Substrate binding and carboxylation by dethiobiotin synthetase--a kinetic and X-ray study. Alexeev, D., Baxter, R.L., Smekal, O., Sawyer, L. Structure (1995) [Pubmed]
WikiGenes - Universities