Artificial Peptidase with an Active Site Comprising a Cu(II) Center and a Proximal Guanidinium Ion. A Carboxypeptidase A Analogue

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• 作者：Junghun Suh and Sung-Ju Moon
• 刊名：Inorganic Chemistry
• 出版年：2001
• 出版时间：September 10, 2001
• 年：2001
• 卷：40
• 期：19
• 页码：4890 - 4895
• 全文大小：80K
• 年卷期：v.40,no.19(September 10, 2001)
• ISSN：1520-510X

文摘

An immobile artificial metallopeptidase having a well-defined active site was constructed on the backbone ofcross-linked polystyrene by adjoining a guanidinium moiety to the Cu(II) complex of a tetraaza ligand. Thecatalyst (CABP) and intermediate polymers were characterized by elemental analysis, IR, inductively coupledplasma measurement, electron probe microanalysis, test for primary amines, binding of Cu(II) ion, and complexationof p-nitrobenzoate ion. CABP effectively catalyzed amide hydrolysis of carboxyl-containing N-acyl amino acids.The catalytic rate of CABP in the hydrolysis of unactivated amides was comparable to that of the catalytic antibodywith the highest peptidase activity reported to date. It is proposed that the guanidinium moiety of CABP recognizesthe carboxylate anion of the substrate whereas the Cu(II) center participates in the cleavage of the amide bond ofthe complexed substrate. Several characteristic features of carboxypeptidase A were reproduced by CABP: catalyticaction of the metal ion, participation of guanidinium in substrate recognition, hydrolysis of small unactivatedamides, and substrate selectivity toward amide bonds adjacent to a carboxylate group.