Characterization of a bifunctional catalase-peroxidase of Burkholderia cenocepacia

Charalabous, Panagoula, Risk, Janet M ORCID: 0000-0002-8770-7783, Jenkins, Rosalind, Birss, Andrew J, Hart, C Anthony and Smalley, John W (2007) Characterization of a bifunctional catalase-peroxidase of Burkholderia cenocepacia. FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY, 50 (1). pp. 37-44.

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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.

Item Type:	Article
Additional Information:	Journal Article Research Support, Non-U.S. Gov't England ## TULIP Type: Articles/Papers (Journal) ##
Uncontrolled Keywords:	catalase-peroxidase, Burkholderia cenocepacia, cystic fibrosis
Subjects:	?? RK ??
Divisions:	Faculty of Health and Life Sciences > Institute of Life Courses and Medical Sciences > School of Dentistry
Depositing User:	Symplectic Admin
Date Deposited:	30 Mar 2009 10:49
Last Modified:	15 Dec 2022 07:09
DOI:	10.1111/j.1574-695X.2007.00224.x
Publisher's Statement :	© 2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved. Please acknowledge that this article has been published in the journal FEMS Immunology & Medical Microbiology. http://dx.doi.org/10.1111/j.1574-695X.2007.00224.x. The definitive version is available at www.blackwell-synergy.com.
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/1107