http://purl.uniprot.org/citations/2935393 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2935393 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2935393 | http://www.w3.org/2000/01/rdf-schema#comment | "The two alcohol dehydrogenases found in Zymomonas mobilis have each been purified using dye-ligand chromatography and affinity elution with nucleotides. The isoenzyme with lower electrophoretic mobility (ZADH-1) is a zinc enzyme with properties essentially similar to preparations described elsewhere. The faster isoenzyme (ZADH-2) accounted for some 90% of the ethanol-oxidizing activity in freshly prepared extracts and corresponded to the iron-activated enzyme previously described. This enzyme was inactivated by zinc; activity could only be retained during purification by including either ferrous ions or cobaltous ions in the buffers. ZADH-2 has relatively low acetaldehyde reductase activity; consequently ZADH-1 is responsible for about half of the physiological activity (acetaldehyde reduction) in Zymomonas cells. Kinetic studies showed that ZADH-2 is activated by ethanol in both reaction directions; a hypothesis for the mechanism of activation is presented. Metal ion analyses of ZADH-2 prepared in the presence of iron or cobalt indicated one atom of the relevant metal per subunit, with no significant zinc content. N-terminal sequence analyses showed that the ZADH-1 has some homology with the Bacillus stearothermophilus enzyme, whereas ZADH-2 resembles the yeast enzyme more closely."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1986.tb09366.x"xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1986.tb09366.x"xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/author | "Scopes R.K."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/author | "Scopes R.K."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/author | "Kelly J.M."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/author | "Kelly J.M."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/author | "Neale A.D."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/author | "Neale A.D."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/author | "Wettenhall R.E.H."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/author | "Wettenhall R.E.H."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/date | "1986"xsd:gYear |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/date | "1986"xsd:gYear |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/pages | "119-124"xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/pages | "119-124"xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/title | "The two alcohol dehydrogenases of Zymomonas mobilis. Purification by differential dye ligand chromatography, molecular characterisation and physiological roles."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/title | "The two alcohol dehydrogenases of Zymomonas mobilis. Purification by differential dye ligand chromatography, molecular characterisation and physiological roles."xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/volume | "154"xsd:string |
http://purl.uniprot.org/citations/2935393 | http://purl.uniprot.org/core/volume | "154"xsd:string |
http://purl.uniprot.org/citations/2935393 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2935393 |
http://purl.uniprot.org/citations/2935393 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2935393 |