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Escherichia coli mutants with a temperature-sensitive alcohol dehydrogenase
Author(s) -
William H. Lorowitz,
David P. Clark
Publication year - 1982
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.152.2.935-938.1982
Subject(s) - alcohol dehydrogenase , escherichia coli , mutant , biology , alcohol oxidoreductase , acetaldehyde , adh1b , alcohol , aldehyde dehydrogenase , biochemistry , allyl alcohol , ethanol , dehydrogenase , enzyme , microbiology and biotechnology , branched chain alpha keto acid dehydrogenase complex , gene , nad+ kinase , catalysis
Mutants of Escherichia coli resistant to allyl alcohol were selected. Such mutants were found to lack alcohol dehydrogenase. In addition, mutants with temperature-sensitive alcohol dehydrogenase activity were obtained. These mutations, designated adhE, are all located at the previously described adh regulatory locus. Most adhE mutants were also defective in acetaldehyde dehydrogenase activity.

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