Enterococcus faecalis heme-dependent catalase
(2002) In Journal of Bacteriology 184(22). p.6351-6356- 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 muM hemin was... (More)
- 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 muM 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/324764
- author
- Frankenberg, Lena LU ; Brugna, Myriam LU and Hederstedt, Lars LU
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Bacteriology
- volume
- 184
- issue
- 22
- pages
- 6351 - 6356
- publisher
- American Society for Microbiology
- external identifiers
-
- wos:000178916700029
- pmid:12399505
- scopus:0036842062
- ISSN
- 0021-9193
- DOI
- 10.1128/JB.184.22.6351-6356.2002
- language
- English
- LU publication?
- yes
- id
- 113648e1-daa5-494c-aa73-afda5503223d (old id 324764)
- date added to LUP
- 2016-04-01 11:58:57
- date last changed
- 2022-01-26 21:06:09
@article{113648e1-daa5-494c-aa73-afda5503223d,
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 muM 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.}},
author = {{Frankenberg, Lena and Brugna, Myriam and Hederstedt, Lars}},
issn = {{0021-9193}},
language = {{eng}},
number = {{22}},
pages = {{6351--6356}},
publisher = {{American Society for Microbiology}},
series = {{Journal of Bacteriology}},
title = {{Enterococcus faecalis heme-dependent catalase}},
url = {{http://dx.doi.org/10.1128/JB.184.22.6351-6356.2002}},
doi = {{10.1128/JB.184.22.6351-6356.2002}},
volume = {{184}},
year = {{2002}},
}