Thermodynamic analysis of small ligand binding to the Escherichia coli repressor of biotin biosynthesis

Biochemistry
Y XuDorothy Beckett

Abstract

BirA is the transcriptional repressor of biotin biosynthesis and a biotin holoenzyme synthetase. It catalyzes synthesis of biotinyl-5'-AMP from the substrates biotin and ATP. The adenylate is the activated intermediate in the biotin transfer reaction as well as the positive allosteric effector for site-specific DNA binding. The affinity of BirA for the adenylate is considerably greater than its affinity for biotin, and both binding reactions are coupled to changes in the conformation of the protein. The temperature dependencies of the two binding interactions have been determined using kinetic techniques. Van't Hoff analysis of the equilibrium dissociation constants derived from the kinetic data indicate that while the two binding processes are characterized by large negative enthalpies, the entropic contributions are small for both. Binding enthalpies have also been determined by isothermal titration calorimetry. Consistent with the results of the van't Hoff analyses, the calorimetric enthalpies are large and negative. The greater precision of the calorimetric measurements allowed more accurate estimation of the entropic contributions to the binding processes, which are of opposite sign for the two ligands. In addition, the he...Continue Reading

References

Sep 22, 1995·Journal of Molecular Biology·J Gómez, E Freire

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Citations

Feb 1, 1997·Current Opinion in Biotechnology·M L Doyle
Dec 1, 1996·Current Opinion in Structural Biology·Y Lindqvist, G Schneider
May 5, 2000·Biomolecular Engineering·A Chapman-Smith, J E Cronan
Feb 16, 2002·Protein Science : a Publication of the Protein Society·Keehwan KwonDorothy Beckett
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Jul 1, 2011·Biophysical Chemistry·Sudheer TungturDorothy Beckett
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Jan 25, 2005·Journal of Molecular Biology·Lihua JinJannette Carey
Mar 4, 1999·The Journal of Nutrition·A Chapman-Smith, J E Cronan

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