Ala226, to Gly and Ser189 to Asp mutations convert rat chymotrypsin B to a trypsin-like protease

Protein Engineering, Design and Selection

Volumn 17, Issue 2, 2004, Pages 127-131

  Jelinek, Balázs ^a   Antal, József ^a   Venekei, István ^a   Gráf, László ^a  

^a EÖTVÖS LORÁND UNIVERSITY   (Hungary)

Author keywords

Autoactivation; Serine protease; Substrate specificity

Indexed keywords

ALANINE 226; AMINO ACID; ASPARTIC ACID; CHYMOTRYPSIN B; GLYCINE; OLIGOPEPTIDE; PANCREAS ENZYME; SERINE 189; SERINE PROTEINASE; TRYPSIN; TRYPSINOGEN; TRYPTASE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; KINETICS; MUTATION; NONHUMAN; PARAMETER; PRIORITY JOURNAL; RAT;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; ASPARTIC ACID; BENZAMIDINES; CHYMOTRYPSIN; CHYMOTRYPSINOGEN; GLYCINE; KINETICS; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE HYDROLASES; PROTEIN CONFORMATION; RATS; SERINE; SUBSTRATE SPECIFICITY; TRYPSIN; TRYPSIN INHIBITORS;

EID: 1842765652     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/gzh014     Document Type: Article

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