Biochemical Journal · 1991 · 45 citations · 22 references
Life SciencesBiochemistryMolecular BiologyEnzyme MechanismEnzymologyMetabolismCatalytic MechanismsCatalytic Residue FunctionEnzyme AssaysEnzyme KineticsEnzyme-substrate RecognitionAldehyde Dehydrogenase CatalysisCatalytic Residue IdentificationDigestionEsterase ActivityFractionationNucleophile ReactivityNucleophilic CatalysisNucleophilic Reactivity
Sheep liver cytoplasmic aldehyde dehydrogenase was labelled by reaction with the substrate p-nitrophenyl di[14C]methylcarbamate. After tryptic digestion and peptide fractionation the labelled residue was identified as Cys-302. This is the first unequivocal identification of the essential enzymic nucleophile in the esterase activity of aldehyde dehydrogenase. By implication, Cys-302 is probably also the residue that is acylated by aldehyde substrates and the first residue that is modified by disulfiram.
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Active site of human liver aldehyde dehydrogenase
Darryl P. Abriola, Robert Fields, Stanley J. Stein et al. · Biochemistry · 1987 · 102 citations
Darin E. Jones, M D Brennan, J Hempel et al. · Proceedings of the National Academy of Sciences · 1988 · 90 citations · Full text