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Study on Substrate Specificity at Subsites for Severe Acute Respiratory Syndrome coronavirus 3cl protease

Acta Biochimica et Biophysica Sinica 2005年第12期37卷 807-813页

作者： Yu-Fei SHAN~1 Gen-Jun XU~(1,2)1 Institute of Bichemistry and Cell Biology.Shanghai Institutes for Biological Sciences,Chinese Academy of Sciences,Shanghai 200031,China 2 College of Life Science Zhejiang Sci-Tech University,Hangzhou 310018,China Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences Shanghai 200031 China.

Autocleavage assay and peptide-based cleavage assay were used to study the substratespecificity of 3cl protease from the severe acute respiratory syndrome *** was found that therecognition between the enzyme and its substrates involved many positions in the substrate,at least includingresidues from P4 to P2′.The deletion of either P4 or P2′residue in the substrate would decrease its cleavageefficiency *** contrast to the previous suggestion that only small residues in substrate could beaccommodated to the S1′subsite,we have found that bulky residues such as Tyr and Trp were also *** addition,based on both peptide-based assay and autocleavage assay,Ile at the P1′position could not behydrolyzed,but the mutant L27A could hydrolyze the Ile peptide *** suggested that there was astereo hindrance between the S1′subsite and the side chain of Ile in the *** 20 amino acids exceptPro could be the residue at the P2′position in the substrate,but the cleavage efficiencies were *** specificity information of the enzyme is helpful for potent anti-virus inhibitor design and usefulfor other coronavirus studies.

关键词： sars coronavirus 3cl protease substrate specificity autocleavage binding site inhibitor design

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