Identification of a catalytically essential nucleophilic residue in sheep liver cytoplasmic aldehyde dehydrogenase
| Autor: | Trevor M. Kitson, Jeremy P. Hill, G G Midwinter |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Cytoplasm
Stereochemistry Molecular Sequence Data Aldehyde dehydrogenase Biochemistry Aldehyde Esterase Residue (chemistry) Nucleophile medicine Animals Trypsin Amino Acid Sequence Cysteine Molecular Biology chemistry.chemical_classification Binding Sites Sheep biology Cell Biology Aldehyde Dehydrogenase Peptide Fragments Enzyme Liver chemistry Disulfiram biology.protein Carbamates Research Article medicine.drug |
| Zdroj: | Biochemical Journal. 275:207-210 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2750207 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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