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Scholarly Communication

Characterisation of a Bi-functional Catalase-peroxidase of Burkholderia cenocepacia

Charalabous, Panagoula; Risk, Janet M.; Jenkins, Rosalind; Birss, Andrew J.; Hart, C. Anthony and Smalley, John W. (2007) Characterisation of a Bi-functional Catalase-peroxidase of Burkholderia cenocepacia. FEMS Immunology and Medical Microbiology, 50 (1). pp. 37-44. ISSN Online: 1574-695X; Print: 0928-8244

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Isolates of Burkholderia cenocepacia express a putative haem-binding protein (Mr 97kDa) which displays intrinsic peroxidase activity. Its role has been re-evaluated, and we now show that it is a bi-functional 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 E. 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). Mass spectrometric analysis indicated that the initial katG translation product may be post-translationally modified in B. cenocepacia to give rise to the mature 97kDa catalase-peroxidase.

Item Type:Article
Additional Information:Published Online: 16 Mar 2007
Uncontrolled Keywords:catalase-peroxidase; Burkholderia cenocepacia; cystic fibrosis
Subjects:R Medicine > RK Dentistry
Departments, Research Centres and Related Units:Academic Faculties, Institutes and Research Centres > Faculty of Medicine > School of Dental Sciences
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. The definitive version is available at
ID Code:1107
Deposited On:30 Mar 2009 11:49
Last Modified:27 Mar 2012 09:39

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