Subsite specificity studies on the unusual cysteine protease clostripain: Charged residues in the P3 position indicate a narrow subsite region

Biological Chemistry

Volumn 378, Issue 10, 1997, Pages 1193-1198

  Bordusa, Frank ^a   Ullmann, Dirk ^a   Jakubke, Hans Dieter ^a  

^a UNIVERSITY OF LEIPZIG   (Germany)

Author keywords

Acyl transfer; Bioorganic chemistry; Enzyme specificity; Protease catalysis

Indexed keywords

ARGININE; CLOSTRIPAIN; DIPEPTIDE; LYSINE;

ARTICLE; CLOSTRIDIUM HISTOLYTICUM; CONTROLLED STUDY; DEACYLATION; ELECTRICITY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HYDROLYSIS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; STEADY STATE;

ACYLATION; ARGININE; BINDING SITES; CATALYSIS; CYSTEINE ENDOPEPTIDASES; DIPEPTIDES; ESTERS; KINETICS; LYSINE; SUBSTRATE SPECIFICITY;

CLOSTRIDIUM HISTOLYTICUM;

EID: 0030688025     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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