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Characterization of a bifunctional catalase–peroxidase of Burkholderia cenocepacia

  1. Panagoula Charalabous1,
  2. Janet M. Risk2,
  3. Rosalind Jenkins3,
  4. Andrew J. Birss1,
  5. C. Anthony Hart4,
  6. John W. Smalley1

Article first published online: 16 MAR 2007

DOI: 10.1111/j.1574-695X.2007.00224.x

Issue

FEMS Immunology & Medical Microbiology

FEMS Immunology & Medical Microbiology

Volume 50, Issue 1, pages 37–44, June 2007

Additional Information

How to Cite

Charalabous, P., Risk, J. M., Jenkins, R., Birss, A. J., Hart, C. A. and Smalley, J. W. (2007), Characterization of a bifunctional catalase–peroxidase of Burkholderia cenocepacia. FEMS Immunology & Medical Microbiology, 50: 37–44. doi: 10.1111/j.1574-695X.2007.00224.x

Author Information

  1. 1

    Microbiology, The University of Liverpool, Liverpool, UK

  2. 2

    Molecular Genetics and Oncology Groups, School of Dental Sciences, The University of Liverpool, Liverpool, UK

  3. 3

    Biomedical Sciences Proteomics Facility, Department of Pharmacology and Therapeutics, The University of Liverpool Street, Liverpool, UK

  4. 4

    Department of Medical Microbiology and Genito-Urinary Medicine, The University of Liverpool, Liverpool, UK

*Correspondence: John W Smalley, School of Dental Sciences, The University of Liverpool, Daulby Street, Liverpool L69 3GN, UK. Tel.: +44 151 706 5272; fax: +44 151 706 5809; e-mail: josmall@liv.ac.uk

Publication History

  1. Issue published online: 16 MAR 2007
  2. Article first published online: 16 MAR 2007
  3. Received 12 July 2006; revised 12 January 2007; accepted 13 January 2007.First published online 16 March 2007.

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Keywords:

  • catalase–peroxidase;
  • Burkholderia cenocepacia;
  • cystic fibrosis

Abstract

Isolates of Burkholderia cenocepacia express a putative haem-binding protein (molecular mass 97 kDa) that displays intrinsic peroxidase activity. Its role has been re-evaluated, and we now show that it is a bifunctional catalase–peroxidase, with activity against tetramethylbenzidine (TMB), o-dianisidine, pyrogallol, and 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulphonic) acid (ABTS). Both peroxidase and catalase activities are optimal at pH 5.5–6.0. The gene encoding this enzyme was cloned and expressed in Escherichia coli. We have named it katG because of its similarity to other katGs, including that from Burkholderia pseudomallei. It is substantially similar to a previously described catalase–peroxidase of B. cenocepacia (katA). MS analysis indicated that the initial katG translation product may be post-translationally modified in B. cenocepacia to give rise to the mature 97-kDa catalase–peroxidase.

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