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• W1972959819 abstract "Chemical modification studies have previously indicated that the S1 binding site of carboxypeptidase Y contains a cysteinyl residue and that the S 1 ′ binding site contains a methionyl residue (Carlsberg Res. Commun. 48, 9–19 (1983); 49, 535–554 (1984); 49, 627–638 (1984)). These studies also indicated that the active site contained an additional methionyl residue situated in an as yet unidentified position. In the present paper the positions of these amino acid residues has been identified in the amino acid sequence which has been revised on the basis of the nucleotide sequence (T. Stevens, personal communications). The cysteinyl residue was identified as Cys-341 after alkylation with14C-iodoacetic acid followed by separation of the peptides produced by cyanogen bromide cleavage and Edman degradation of the radioactive peptide. The methionyl residue situated in the S 1 ′ binding site was identified as Met-398 after alkylation with14C-iodoacetamide, separation of the peptides produced by cyanogen bromide cleavage and thermal cleavage of the peptide containing the radioactivity. This assignment was confirmed by the failure of cyanogen bromide to cleave at the position of carboxypeptidase Y in which this particular methionyl residue had been alkylated or oxidized. Using the same method the other methionyl residue in the active site was identified as Met-313." @default.
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• W1972959819 creator A5049835003 @default.
• W1972959819 date "1984-01-01" @default.
• W1972959819 modified "2023-09-23" @default.
• W1972959819 title "Identification of methionyl and cysteinyl residues in the substrate binding site of carboxypeptidase Y" @default.
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• W1972959819 doi "https://doi.org/10.1007/bf02907496" @default.
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