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Mutagenesis of Recombinant Human Fibroblast Stromelysin C-Terminus Reveals the Autodegradation Pathway

MW Qoronfleh,T Ho,T Banks,T Pulvino,P Brake,R Ciccarelli, J Koehn, J Huang,R Wahl

Protein & peptide letters/Protein and peptide letters(1996)

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摘要
Stromelysin as a member of the matrix metalloproteinases (MMP) family participates in connective tissue remodeling and diseases. Understanding MMPs' catalytic mechanism and designing specific inhibitors to control their activity is of great interest. A clone for mature truncated stromelysin (SL), F83 to T260, without the C-terminal hemopexin-like domain was constructed a d expressed in E. coli. The purified, recombinant protein was active and had a specific activity and Ki values comparable to that of the native enzyme. However, protein degradation was observed which was attributed to autolysis. A specific autolytic site at S244-L245 was identified by N-terminal sequencing. A series of SL muteins and new truncations were engineered to evaluate their effects on autolysis. The replacement of L245 with an R prevents the autodegradation of SL at the S244-L245 autolytic site. This substitution reveals the primary site initiating SL autolysis (self-catalyzed cleavage) and locates it at Vl63-L164.
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