Journal Article

Characterization of a bifunctional catalase–peroxidase of <i>Burkholderia cenocepacia</i>

Panagoula Charalabous, Janet M. Risk, Rosalind Jenkins, Andrew J. Birss, C. Anthony Hart and John W. Smalley

in FEMS Immunology & Medical Microbiology

Published on behalf of Federation of Microbiological Societies

Volume 50, issue 1, pages 37-44
Published in print June 2007 | ISSN: 0928-8244
Published online March 2007 | e-ISSN: 1574-695X | DOI: http://dx.doi.org/10.1111/j.1574-695X.2007.00224.x
Characterization of a bifunctional catalase–peroxidase of Burkholderia cenocepacia

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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.

Keywords: catalase–peroxidase; Burkholderia cenocepacia; cystic fibrosis

Journal Article.  4265 words.  Illustrated.

Subjects: Medical Microbiology and Virology ; Biotechnology ; Genetics and Genomics ; Microbiology ; Molecular and Cell Biology

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