Applications of molecular biology to study aldehyde dehydrogenase.
Liver mitochondrial aldehyde dehydrogenase has been cloned and expressed in E. coli as the mature or the precursor form. This has allowed for site directed mutagenesis to be performed to study active site components of the enzyme. Residues investigated were cysteine, histidines and a glutamate. The import of the precursor into mitochondria in the presence and absence of added alcohols was investigated. Alcohols, in a dose dependent manner, inhibited the import of the precursor into isolated rat liver mitochondria.
Weiner
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Department of Biochemistry, Purdue University, West Lafayette, IN 47907-1153, USA.
D000438:Alcohols / Q000633:toxicity; D000444:Aldehyde Dehydrogenase / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D002417:Cattle; D003001:Cloning, Molecular; D004792:Enzyme Precursors / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D008930:Mitochondria, Liver / Q000187:drug effects / Q000201:enzymology; D008967:Molecular Biology; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D021382:Protein Sorting Signals / Q000235:genetics; D051381:Rats
D000438:Alcohols; D004792:Enzyme Precursors; D021382:Protein Sorting Signals; D000444:Aldehyde Dehydrogenase