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Article: Hydrogen peroxide produced by two amino acid oxidases mediates antibacterial actions

TitleHydrogen peroxide produced by two amino acid oxidases mediates antibacterial actions
Authors
Issue Date2004
PublisherHan-Gug Misaengmul Hag-hoe. The Journal's web site is located at http://www.msk.or.kr/jm/jmhome.htm
Citation
Journal Of Microbiology, 2004, v. 42 n. 4, p. 336-339 How to Cite?
AbstractThe antibacterial actions of two amino acid oxidases, a D-amino acid oxidase from hog kidney and a L-amino acid oxidase from the venom of Agkistrodon halys, were investigated, demonstrating that both enzymes were able to inhibit the growth of both Gram-positive and Gram-negative bacteria, and that hydrogen peroxide, a product of their enzymatic reactions, was the antibacterial factor. However, hydrogen peroxide generated in the enzymatic reactions was not sufficient to explain the degree to which bacterial growth was inhibited. A fluorescence labeling assay showed that both of these two enzymes could bind to the surfaces of bacteria. To the best of our knowledge, this is the first report regarding the antibacterial activity of the D-amino acid oxidases.
Persistent Identifierhttp://hdl.handle.net/10722/171727
ISSN
2015 Impact Factor: 1.621
2015 SCImago Journal Rankings: 0.741
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Hen_US
dc.contributor.authorYang, Qen_US
dc.contributor.authorSun, Men_US
dc.contributor.authorTeng, Men_US
dc.contributor.authorNiu, Len_US
dc.date.accessioned2012-10-30T06:16:39Z-
dc.date.available2012-10-30T06:16:39Z-
dc.date.issued2004en_US
dc.identifier.citationJournal Of Microbiology, 2004, v. 42 n. 4, p. 336-339en_US
dc.identifier.issn1225-8873en_US
dc.identifier.urihttp://hdl.handle.net/10722/171727-
dc.description.abstractThe antibacterial actions of two amino acid oxidases, a D-amino acid oxidase from hog kidney and a L-amino acid oxidase from the venom of Agkistrodon halys, were investigated, demonstrating that both enzymes were able to inhibit the growth of both Gram-positive and Gram-negative bacteria, and that hydrogen peroxide, a product of their enzymatic reactions, was the antibacterial factor. However, hydrogen peroxide generated in the enzymatic reactions was not sufficient to explain the degree to which bacterial growth was inhibited. A fluorescence labeling assay showed that both of these two enzymes could bind to the surfaces of bacteria. To the best of our knowledge, this is the first report regarding the antibacterial activity of the D-amino acid oxidases.en_US
dc.languageengen_US
dc.publisherHan-Gug Misaengmul Hag-hoe. The Journal's web site is located at http://www.msk.or.kr/jm/jmhome.htmen_US
dc.relation.ispartofJournal of Microbiologyen_US
dc.subject.meshAgkistrodonen_US
dc.subject.meshAmino Acid Oxidoreductases - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCell Wall - Metabolismen_US
dc.subject.meshD-Amino-Acid Oxidase - Metabolismen_US
dc.subject.meshDown-Regulationen_US
dc.subject.meshGram-Negative Bacteria - Drug Effects - Growth & Development - Metabolismen_US
dc.subject.meshGram-Positive Bacteria - Drug Effects - Growth & Development - Metabolismen_US
dc.subject.meshHydrogen Peroxide - Metabolism - Pharmacologyen_US
dc.subject.meshL-Amino Acid Oxidaseen_US
dc.subject.meshSwineen_US
dc.titleHydrogen peroxide produced by two amino acid oxidases mediates antibacterial actionsen_US
dc.typeArticleen_US
dc.identifier.emailZhang, H:hzhang20@hku.hken_US
dc.identifier.authorityZhang, H=rp00306en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid15650691-
dc.identifier.scopuseid_2-s2.0-12344304974en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-12344304974&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume42en_US
dc.identifier.issue4en_US
dc.identifier.spage336en_US
dc.identifier.epage339en_US
dc.identifier.isiWOS:000226509400011-
dc.publisher.placeKorea, Republic ofen_US
dc.identifier.scopusauthoridZhang, H=7409196101en_US
dc.identifier.scopusauthoridYang, Q=7404076758en_US
dc.identifier.scopusauthoridSun, M=7403180609en_US
dc.identifier.scopusauthoridTeng, M=7101891754en_US
dc.identifier.scopusauthoridNiu, L=7101760477en_US

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