An artificial aspartic proteinase system.
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.
Jiang
Lin
L
Technical Institute of Physics and Chemistry, Chinese Academy of Sciences (CAS), Box 5131, Beijing 100101, PR China.
Liu
Zhilian
Z
Liang
Zhi
Z
Gao
Yunhua
Y
D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D011480:Protease Inhibitors / Q000494:pharmacology; D011487:Protein Conformation; D013379:Substrate Specificity
D011480:Protease Inhibitors; D016282:Aspartic Acid Endopeptidases