Bacterial [Cu,Zn]-superoxide dismutase : phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!
Copper- and zinc-containing superoxide dismutases ([Cu,Zn]-SODs) are generally considered almost exclusively eukaryotic enzymes, protecting the cytosol and extracellular compartments of higher organisms from damage by oxygen free-radicals. The recent description of a few examples of bacterial forms of the enzyme, located in the periplasm of different Gram-negative micro-organisms, prompted a re-evaluation of this general perception. A PCR-based approach has been developed and used successfully to identify bacterial genes encoding [Cu,Zn]-SOD in a wide range of important human and animal pathogens-members of the Haemophilus, Actinobacillus and Pasteurella (HAP) group, and Neisseria meningitidis. Comparison of [Cu,Zn]-SOD peptide sequences found in Haemophilus ducreyi, Actinobacillus pleuropneumoniae, Actinobacillus actinomycetemcomitans, Pasteurella multocida, and N. meningitidis with previously described bacterial proteins and examples of eukaryotic [Cu,Zn]-SOD has shown that the bacterial proteins constitute a distinct family apparently widely separated in evolutionary terms from the eukaryotic examples. The widespread occurrence of [Cu,Zn]-SOD in the periplasm of bacterial pathogens, appropriately located to dismute exogenously derived superoxide radical anions, suggests that this enzyme may play a role in the interactive biology of organisms with their hosts and so contribute to their capacity to cause disease.
Medienart: |
Artikel |
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Erscheinungsjahr: |
1995 |
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Erschienen: |
1995 |
Enthalten in: |
Zur Gesamtaufnahme - volume:141 ( Pt 9) |
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Enthalten in: |
Microbiology (Reading, England) - 141 ( Pt 9)(1995) vom: 08. Sept., Seite 2271-9 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Kroll, J S [VerfasserIn] |
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Themen: |
789U1901C5 |
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Anmerkungen: |
Date Completed 16.01.1996 Date Revised 26.08.2020 published: Print GENBANK: X83122, X83123, X83124, X83125, X83126 Citation Status MEDLINE |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM074732048 |
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100 | 1 | |a Kroll, J S |e verfasserin |4 aut | |
245 | 1 | 0 | |a Bacterial [Cu,Zn]-superoxide dismutase |b phylogenetically distinct from the eukaryotic enzyme, and not so rare after all! |
264 | 1 | |c 1995 | |
336 | |a Text |b txt |2 rdacontent | ||
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338 | |a Band |b nc |2 rdacarrier | ||
500 | |a Date Completed 16.01.1996 | ||
500 | |a Date Revised 26.08.2020 | ||
500 | |a published: Print | ||
500 | |a GENBANK: X83122, X83123, X83124, X83125, X83126 | ||
500 | |a Citation Status MEDLINE | ||
520 | |a Copper- and zinc-containing superoxide dismutases ([Cu,Zn]-SODs) are generally considered almost exclusively eukaryotic enzymes, protecting the cytosol and extracellular compartments of higher organisms from damage by oxygen free-radicals. The recent description of a few examples of bacterial forms of the enzyme, located in the periplasm of different Gram-negative micro-organisms, prompted a re-evaluation of this general perception. A PCR-based approach has been developed and used successfully to identify bacterial genes encoding [Cu,Zn]-SOD in a wide range of important human and animal pathogens-members of the Haemophilus, Actinobacillus and Pasteurella (HAP) group, and Neisseria meningitidis. Comparison of [Cu,Zn]-SOD peptide sequences found in Haemophilus ducreyi, Actinobacillus pleuropneumoniae, Actinobacillus actinomycetemcomitans, Pasteurella multocida, and N. meningitidis with previously described bacterial proteins and examples of eukaryotic [Cu,Zn]-SOD has shown that the bacterial proteins constitute a distinct family apparently widely separated in evolutionary terms from the eukaryotic examples. The widespread occurrence of [Cu,Zn]-SOD in the periplasm of bacterial pathogens, appropriately located to dismute exogenously derived superoxide radical anions, suggests that this enzyme may play a role in the interactive biology of organisms with their hosts and so contribute to their capacity to cause disease | ||
650 | 4 | |a Comparative Study | |
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
650 | 7 | |a Bacterial Proteins |2 NLM | |
650 | 7 | |a Copper |2 NLM | |
650 | 7 | |a 789U1901C5 |2 NLM | |
650 | 7 | |a Superoxide Dismutase |2 NLM | |
650 | 7 | |a EC 1.15.1.1 |2 NLM | |
650 | 7 | |a Zinc |2 NLM | |
650 | 7 | |a J41CSQ7QDS |2 NLM | |
700 | 1 | |a Langford, P R |e verfasserin |4 aut | |
700 | 1 | |a Wilks, K E |e verfasserin |4 aut | |
700 | 1 | |a Keil, A D |e verfasserin |4 aut | |
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