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Journal articles on the topic 'Dethiobiotin synthetase'

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Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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1

Sandalova, Tatyana, Gunter Schneider, Helena Käck, and Ylva Lindqvist. "Structure of dethiobiotin synthetase at 0.97 Å resolution." Acta Crystallographica Section D Biological Crystallography 55, no. 3 (March 1, 1999): 610–24. http://dx.doi.org/10.1107/s090744499801381x.

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2

Salaemae, Wanisa, Min Y. Yap, Kate L. Wegener, Grant W. Booker, Matthew C. J. Wilce, and Steven W. Polyak. "Nucleotide triphosphate promiscuity in Mycobacterium tuberculosis dethiobiotin synthetase." Tuberculosis 95, no. 3 (May 2015): 259–66. http://dx.doi.org/10.1016/j.tube.2015.02.046.

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3

Alexeev, Dmitriy, Robert L. Baxter, and Lindsay Sawyer. "Mechanistic implications and family relationships from the structure of dethiobiotin synthetase." Structure 2, no. 11 (November 1994): 1061–72. http://dx.doi.org/10.1016/s0969-2126(94)00109-x.

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4

Porebski, Przemyslaw J., Maria Klimecka, Maksymilian Chruszcz, Robert A. Nicholls, Krzysztof Murzyn, Marianne E. Cuff, Xiaohui Xu, et al. "Structural characterization of Helicobacter pylori dethiobiotin synthetase reveals differences between family members." FEBS Journal 279, no. 6 (February 27, 2012): 1093–105. http://dx.doi.org/10.1111/j.1742-4658.2012.08506.x.

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5

Rendina, Alan R., Wendy S. Taylor, Katharine Gibson, George Lorimer, Dennis Rayner, Bruce Lockett, Kevin Kranis, et al. "The design and synthesis of inhibitors of dethiobiotin synthetase as potential herbicides." Pesticide Science 55, no. 3 (March 1999): 236–47. http://dx.doi.org/10.1002/(sici)1096-9063(199903)55:3<236::aid-ps888>3.0.co;2-0.

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6

Käck, Helena, Jenny Sandmark, Gunter Schneider, Ylva Lindqvist, and Katharine J. Gibson. "Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis." Protein Science 7, no. 12 (December 1998): 2560–66. http://dx.doi.org/10.1002/pro.5560071209.

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7

Thompson, Andrew P., Kate L. Wegener, Grant W. Booker, Steven W. Polyak, and John B. Bruning. "Precipitant–ligand exchange technique reveals the ADP binding mode inMycobacterium tuberculosisdethiobiotin synthetase." Acta Crystallographica Section D Structural Biology 74, no. 10 (October 1, 2018): 965–72. http://dx.doi.org/10.1107/s2059798318010136.

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Abstract:
Dethiobiotin synthetase fromMycobacterium tuberculosis(MtDTBS) is a promising antituberculosis drug target. Small-molecule inhibitors that targetMtDTBS provide a route towards new therapeutics for the treatment of antibiotic-resistant tuberculosis. Adenosine diphosphate (ADP) is an inhibitor ofMtDTBS; however, structural studies into its mechanism of inhibition have been unsuccessful owing to competitive binding to the enzyme by crystallographic precipitants such as citrate and sulfate. Here, a crystallographic technique termed precipitant–ligand exchange has been developed to exchange protein-bound precipitants with ligands of interest. Proof of concept for the exchange method was demonstrated using cytidine triphosphate (CTP), which adopted the same binding mechanism as that obtained with traditional crystal-soaking techniques. Precipitant–ligand exchange also yielded the previously intractable structure ofMtDTBS in complex with ADP solved to 2.4 Å resolution. This result demonstrates the utility of precipitant–ligand exchange, which may be widely applicable to protein crystallography.
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8

Huang, Weijun, Ylva Lindqvist, Gunter Schneider, Katharine J. Gibson, Dennis Flint, and George Lorimer. "Crystal structure of an ATP-dependent carboxylase, dethiobiotin synthetase, at 1.65 å resolution." Structure 2, no. 5 (May 1994): 407–14. http://dx.doi.org/10.1016/s0969-2126(00)00042-3.

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9

Alexeev, Dmitriy, Robert L. Baxter, Otto Smekal, and Lindsay Sawyer. "Substrate binding and carboxylation by dethiobiotin synthetase — a kinetic and X-ray study." Structure 3, no. 11 (November 1995): 1207–15. http://dx.doi.org/10.1016/s0969-2126(01)00256-8.

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10

Baxter, Robert L., and Helen C. Baxter. "The mechanism of Escherichia coli dethiobiotin synthetase—the closure of the ureido ring of dethiobiotin involves formation of a carbamic-phosphate mixed anhydride." J. Chem. Soc., Chem. Commun., no. 6 (1994): 759–60. http://dx.doi.org/10.1039/c39940000759.

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11

Dey, Sanghamitra, James M. Lane, Richard E. Lee, Eric J. Rubin, and James C. Sacchettini. "Structural Characterization of theMycobacterium tuberculosisBiotin Biosynthesis Enzymes 7,8-Diaminopelargonic Acid Synthase and Dethiobiotin Synthetase,." Biochemistry 49, no. 31 (August 10, 2010): 6746–60. http://dx.doi.org/10.1021/bi902097j.

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12

Gibson, Katharine J., George H. Lorimer, Alan R. Rendina, Wendy S. Taylor, Gerald Cohen, Anthony A. Gatenby, William G. Payne, D. Christopher Roe, and Bruce A. Lockett. "Dethiobiotin Synthetase: The Carbonylation of 7,8-Diaminononanoic Acid Proceeds Regiospecifically via the N7-Carbamate." Biochemistry 34, no. 35 (September 5, 1995): 10976–84. http://dx.doi.org/10.1021/bi00035a003.

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13

Alexeev, D., S. M. Bury, C. W. G. Boys, M. A. Turner, L. Sawyer, A. J. Ramsey, H. C. Baxter, and R. L. Baxter. "Sequence and Crystallization of Escherichia coli Dethiobiotin Synthetase, the Penultimate Enzyme of Biotin Biosynthesis." Journal of Molecular Biology 235, no. 2 (January 1994): 774–76. http://dx.doi.org/10.1006/jmbi.1994.1030.

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14

Gibson, Katharine J. "Isolation and Chemistry of the Mixed Anhydride Intermediate in the Reaction Catalyzed by Dethiobiotin Synthetase." Biochemistry 36, no. 28 (July 1997): 8474–78. http://dx.doi.org/10.1021/bi970447t.

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15

Wu, Chwen-Huey, Yu-Yen Bao, Chung-Ping Shao, and David Shiuan. "Molecular cloning and nucleotide sequencing of bioF (7-keto-8-amino pelargonic acid synthetase), BioC and BioD (dethiobiotin synthetase) genes of Erwinia herbicola." IUBMB Life 41, no. 2 (February 1997): 311–15. http://dx.doi.org/10.1080/15216549700201321.

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16

Galperin, Michael Y., and Nick V. Grishin. "The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase." Proteins: Structure, Function, and Genetics 41, no. 2 (2000): 238–47. http://dx.doi.org/10.1002/1097-0134(20001101)41:2<238::aid-prot80>3.0.co;2-l.

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17

Baxter, Robert L., Andrew J. Ramsey, Lisa A. Mclver, and Helen C. Baxter. "Mechanism of dethiobiotin synthetase—characterisation of the 8-aminocarbamate of (7R,8S)-7,8 diaminononanoate as an enzyme-bound intermediate." J. Chem. Soc., Chem. Commun., no. 5 (1994): 559–60. http://dx.doi.org/10.1039/c39940000559.

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18

Huang, Weijun, Jia Jia, Katharine J. Gibson, Wendy S. Taylor, Alan R. Rendina, Gunter Schneider, and Ylva Lindqvist. "Mechanism of an ATP-Dependent Carboxylase, Dethiobiotin Synthetase, Based on Crystallographic Studies of Complexes with Substrates and a Reaction Intermediate." Biochemistry 34, no. 35 (September 5, 1995): 10985–95. http://dx.doi.org/10.1021/bi00035a004.

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19

Cobessi, David, Renaud Dumas, Virginie Pautre, Céline Meinguet, Jean-Luc Ferrer, and Claude Alban. "Biochemical and Structural Characterization of the Arabidopsis Bifunctional Enzyme Dethiobiotin Synthetase–Diaminopelargonic Acid Aminotransferase: Evidence for Substrate Channeling in Biotin Synthesis." Plant Cell 24, no. 4 (April 2012): 1608–25. http://dx.doi.org/10.1105/tpc.112.097675.

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20

Gibson, Katharine J., George H. Lorimer, Alan R. Rendina, Wendy S. Taylor, Gerald Cohen, Anthony A. Gatenby, William G. Payne, D. Christopher Roe, and Bruce A. Lockett. "Dethiobiotin Synthetase: The Carbonylation of 7,8-Diaminononanoic Acid Proceeds Regiospecifically via the N7-Carbamate. [Erratum to document cited in CA123:137125]." Biochemistry 34, no. 48 (December 1995): 15880. http://dx.doi.org/10.1021/bi00048a034.

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21

Alexeev, Dmitriy, Robert L. Baxter, Dominic J. Campopiano, Robin S. McAlpine, Lisa McIver, and Lindsay Sawyer. "Rational design of an inhibitor of dethiobiotin synthetase; interaction of 6-hydroxypyrimindin-4(3H)-one with the adenine base binding site." Tetrahedron 54, no. 52 (December 1998): 15891–98. http://dx.doi.org/10.1016/s0040-4020(98)00999-5.

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