An artificial aspartic proteinase system.

Lin Jiang; Zhilian Liu; Zhi Liang; Yunhua Gao

doi:10.1016/j.bmc.2005.03.026

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PubMed · 15862996

An artificial aspartic proteinase system.

Lin Jiang·Zhilian Liu·Zhi Liang·Yunhua Gao

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Abstract

A series of aza crown ether derivatives with or without carboxyl groups in their side arms were synthesized and the former showed deacylation activities toward amino acid p-nitrophenyl ester hydrohalides. Substrate-selective phenomena were also observed. The relationship between the structures and deacylation activities of corresponding compounds suggested a nucleophilic catalytic mechanism. The results partially simulate some aspartic proteinases in the case of catalytic mechanism and are also useful for us to understand the detailed catalytic process of aspartic proteinases.

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Aspartic Acid Endopeptidases Catalysis Hydrogen-Ion Concentration Kinetics Magnetic Resonance Spectroscopy Mass Spectrometry Protease Inhibitors Protein Conformation Substrate Specificity Journal Article Research Support, Non-U.S. Gov't

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Lin Jiang, Zhilian Liu, Zhi Liang, Yunhua Gao. 2005-06-01. An artificial aspartic proteinase system.. https://doi.org/10.1016/j.bmc.2005.03.026

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