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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1994-4-4
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pubmed:abstractText |
We 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 metal-catalyzed 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 II. This histidine residue lies 10 residues away from a proposed metal-binding site, H263XXXH267, 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Diethyl Pyrocarbonate,
http://linkedlifedata.com/resource/pubmed/chemical/Dithionitrobenzoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxylamine,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxylamines,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Sugar Alcohol Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/Trinitrobenzenesulfonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/glycerol dehydrogenase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6592-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8120011-Alcohol Dehydrogenase,
pubmed-meshheading:8120011-Amino Acid Sequence,
pubmed-meshheading:8120011-Chromatography, Gel,
pubmed-meshheading:8120011-Chromatography, High Pressure Liquid,
pubmed-meshheading:8120011-Chromatography, Ion Exchange,
pubmed-meshheading:8120011-Consensus Sequence,
pubmed-meshheading:8120011-Diethyl Pyrocarbonate,
pubmed-meshheading:8120011-Dithionitrobenzoic Acid,
pubmed-meshheading:8120011-Escherichia coli,
pubmed-meshheading:8120011-Hydroxylamine,
pubmed-meshheading:8120011-Hydroxylamines,
pubmed-meshheading:8120011-Iron,
pubmed-meshheading:8120011-Isoenzymes,
pubmed-meshheading:8120011-Molecular Sequence Data,
pubmed-meshheading:8120011-Peptide Fragments,
pubmed-meshheading:8120011-Sequence Homology, Amino Acid,
pubmed-meshheading:8120011-Sugar Alcohol Dehydrogenases,
pubmed-meshheading:8120011-Trinitrobenzenesulfonic Acid,
pubmed-meshheading:8120011-Zymomonas
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pubmed:year |
1994
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pubmed:articleTitle |
Metal-catalyzed oxidation of Fe2+ dehydrogenases. Consensus target sequence between propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis.
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pubmed:affiliation |
Departement de Ciències Mèdiques Basiques, Facultat de Medicina, Universitat de Lleida, Spain.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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