Identification of a segment containing a reactive cysteine residue in human liver cytoplasmic aldehyde dehydrogenase (isoenzyme E1).
A single cysteine residue is selectively alkylated by iodoacetamide in cytoplasmic human liver aldehyde dehydrogenase (isoenzyme E1). The amino acid sequence of a 35-residue fragment containing this residue is determined, showing two additional cysteine residues and also three histidine residues. The alkylation is selective for Cys-30 of this fragment, with only little alkylation even at an adjacent residue, Cys-29. The region examined is likely to be of significance in the reaction of this isoenzyme with disulfiram since disulfiram blocks the selective alkylation.
D000444:Aldehyde Dehydrogenase; D000445:Aldehyde Oxidoreductases / Q000032:analysis*; D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D003545:Cysteine / Q000032:analysis*; D007527:Isoenzymes / Q000032:analysis*; D008099:Liver / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis
D007527:Isoenzymes; D010446:Peptide Fragments; D000445:Aldehyde Oxidoreductases; D000444:Aldehyde Dehydrogenase; D003545:Cysteine