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Catalytic activity of -chymotrypsin in which histidine-57 has been methylated.


ABSTRACT: The properties of a derivative of alpha-chymotrypsin in which histidine-57 has been methylated have been examined. Although the modified enzyme binds substrate with the same affinity as does native alpha-chymotrypsin, acylation and deacylation occur at much decreased rates. As for native alpha-chymotrypsin, a basic group of pK(a) approx. 7 is involved in both acylation and deacylation. The significance of these results is considered in relation to the normal function of histidine-57.

SUBMITTER: Henderson R 

PROVIDER: S-EPMC1177107 | biostudies-other | 1971 Aug

REPOSITORIES: biostudies-other

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