Literature DB >> 17244476

Biochemical study of recombinant PcrA from Staphylococcus aureus for the development of screening assays.

Sandy Dubaele1, Christophe Martin, Jacqueline Bohn, Patrick Chène.   

Abstract

Helicases are ubiquitous enzymes, which utilize the energy liberated during nucleotide triphosphate hydrolysis to separate double-stranded nucleic acids into single strands. These enzymes are very attractive targets for the development of new antibacterial compounds. The PcrA DNA helicase from Staphylococcus aureus is a good candidate for drug discovery. This enzyme is unique in the genome of S. aureus and essential for this bacterium. Furthermore, it has recently been published that it is possible to identify inhibitors of DNA helicases such as PcrA. In this report, we study the properties of recombinant PcrA from S. aureus purified from Escherichia coli to develop ATPase and helicase assays to screen for inhibitors.

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Year:  2007        PMID: 17244476     DOI: 10.5483/bmbrep.2007.40.1.007

Source DB:  PubMed          Journal:  J Biochem Mol Biol        ISSN: 1225-8687


  1 in total

1.  Functional analysis of the superfamily 1 DNA helicases encoded by Mycoplasma pneumoniae and Mycoplasma genitalium.

Authors:  Silvia Estevão; Helga U van der Heul; Marcel Sluijter; Theo Hoogenboezem; Nico G Hartwig; Annemarie M C van Rossum; Cornelis Vink
Journal:  PLoS One       Date:  2013-07-23       Impact factor: 3.240

  1 in total

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