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The crystal structures of carboxypeptidase T (CpT) complexes with phenylalanine and arginine substrate analogs – benzylsuccinic acid and (2‐guanidinoethylmercapto)succinic acid – were determined by the molecular replacement method at resolutions of 1.57 Å and 1.62 Å to clarify the broad substrate specificity profile of the enzyme. The conservative Leu211 and Leu254 residues (also present in both carboxypeptidase...
Molecular modeling was addressed to understand different substrate‐binding modes and clarify the role of two positively charged residues of the penicillin G acylase active site – βR263 and αR145 – in binding of negatively charged substrates. Although the electrostatic contribution to productive substrate binding was dominated by βR263 rather than αR145, it was found that productive binding was not...
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