Affiliation:
1. Department of Cell and Organism Biology, Lund University, SE-223 62 Lund, Sweden
Abstract
ABSTRACT
Enterococcus faecalis
cells cannot synthesize porphyrins and do not rely on heme for growth but can take up heme and use it to synthesize heme proteins. We recently described a cytochrome
bd
in
E. faecalis
strain V583 and here report the identification of a chromosomal gene,
katA
, encoding a heme-containing cytoplasmic catalase. The 54-kDa KatA polypeptide shows sequence similarity to members of the family of monofunctional catalases. A hexahistidyl-tagged version of the catalase was purified, and major characteristics of the enzyme were determined. It contains one protoheme IX group per KatA polypeptide. Catalase activity was detected only in
E. faecalis
cells grown in the presence of heme in the medium; about 2 and 10 μM hemin was required for half-maximal and maximal production of catalase, respectively. Our finding of a catalase whose synthesis is dependent on the acquisition of heme in the opportunistic pathogen
E. faecalis
might be of clinical importance. Studies of cellular heme transport and heme protein assembly and in vivo synthesis of metalloprotein analogs for biotechnological applications are impeded by the lack of experimental systems. We conclude that the
E. faecalis
cell potentially provides such a desired system.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
101 articles.
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