Absolute steric course of hydrolysis by. alpha.-chymotrypsin. Esters of. alpha.-benzylsuccinic,. alpha.-methyl-. beta.-phenylpropionic, and. alpha.-methylsuccinic acids
SG Cohen, A Milovanovic
Index: Cohen,S.G.; Milovanovic,A. Journal of the American Chemical Society, 1968 , vol. 90, p. 3495 - 3502
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Citation Number: 60
Abstract
Abstract: The active site of a-chymotrypsin is described in terms of parts complementary to parts of a natural substrate, L-methyl N-acetylphenylalaninate, L-MAPhe, ar, a cavity or fold in which the P-aryl group provides primary binding; a site of small volume, h, contiguous with ar, into which the aH fits; a surface site, am, at which the a-acylamido group associates by hydrogen bonding; and a surface site, n, at which the ester group is hydrolyzed. DL- ...
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