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dc.contributor.authorCabiscol Català, Elisa
dc.contributor.authorAguilar, Juan
dc.contributor.authorRos Salvador, Joaquim
dc.date.accessioned2016-03-30T08:40:19Z
dc.date.available2016-03-30T08:40:19Z
dc.date.issued1994
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/10459.1/56772
dc.description.abstractWe have studied two enzymes of a newly described family of dehydrogenases with high sequence homology, 1,2-propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis. These enzymes perform their metabolic role under anaerobic conditions; in the presence of oxygen, they show a very similar inactivation pattern by a metalcatalyzed oxidation system. Titration of histidine residues with diethyl pyrocarbonate showed one histidine residue less in the oxidized enzymes. Comparison of subtilisin peptide maps of active and inactivated enzymes showed a difference in one histidine-containing peptide, the sequence of which is YNTPH277GVAN for propanediol oxidoreductase and YNLPH277GV for alcohol dehydrogenase 11. This histidine residue lies 10 residues away from a proposed metal-binding site, H263XyXHa67, necessary to explain a site-specific free radical mechanism. The three histidine residues here described are strictly conserved in all enzymes of this family. In this report we propose that histidine 277 is a target for oxidation by a metal-catalyzed oxidation system and that this modification leads to the irreversible inactivation of both enzymes.ca_ES
dc.language.isoengca_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biologyca_ES
dc.relation.isformatofReproducció del document publicat a http://www.jbc.org/content/269/9/6592.full.pdfca_ES
dc.relation.ispartofJournal of Biological Chemistry, 1994, Vol. 269, núm. 9, p. 6592-6597ca_ES
dc.rights(c) The American Society for Biochemistry and Molecular Biology, 1994ca_ES
dc.titleMetal-catalyzed Oxidation of Fe2+ Dehydrogenases: consensus target sequence between Propanediol Oxidoreductase of Escherichia Coli and alcohol dehydrogenase I1 of Zymomonas Mobilisca_ES
dc.typearticleca_ES
dc.identifier.idgrec002930
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES


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