Stereoselectivity in Peptide Hydrolysis by Chiral Dizinc Complexes
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چکیده
منابع مشابه
A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase.
The active sites of aminopeptidase A (PepA) from Escherichia coli and leucine aminopeptidase from bovine lens are isostructural, as shown by x-ray structures at 2.5 A and 1.6 A resolution, respectively. In both structures, a bicarbonate anion is bound to an arginine side chain (Arg-356 in PepA and Arg-336 in leucine aminopeptidase) very near two catalytic zinc ions. It is shown that PepA is act...
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In order to gain a more detailed insight into the relationship between substrate structure and the stereoselectivity of the enzyme pig liver esterase (E.C. 3.1.1 .I .) a large series of mainly meso and prochiral diesters with an open chain or a cyclic structure has been studied and evaluated. Results obtained with 3substituted cyclopropane-l,2-dicarboxylates are incompatible with the three-dime...
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ژورنال
عنوان ژورنال: Journal of Computer Chemistry, Japan
سال: 2015
ISSN: 1347-1767,1347-3824
DOI: 10.2477/jccj.2015-0028