Identification of a catalytically essential nucleophilic residue in sheep liver cytoplasmic aldehyde dehydrogenase

Trevor M. Kitson, Jeremy P. Hill, Graeme G. Midwinter

Biochemical Journal · 1991 · 45 citations · 22 references

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Abstract

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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