Abstract
CHEMICAL modifications of enzymes have generally been used to identify catalytically functional amino-acid residues. Thus, inactivation with diisopropylphosphofluoridate (DFP) has identified a number of ‘seryl’ enzymes1 and interaction with alkylhalides or paramercuribenzoate (PMB) has defined a group of sulphydryl enzymes2. Similarly, we have used N-acetylimidazole to demonstrate a ‘tyrosyl’ enzyme, carboxypeptidase A (ref. 3).
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RIORDAN, J., WACKER, W. & VALLER, B. ‘Buried’ Tyrosyl Residues and the Activity of Trypsin. Nature 208, 1209–1211 (1965). https://doi.org/10.1038/2081209a0
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DOI: https://doi.org/10.1038/2081209a0
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