Document Detail

Kinetics and mechanism of catalysis by proteolytic enzymes. A comparison of the kinetics of hydrolysis of synthetic substrates by bovine alpha- and beta-trypsin.
MedLine Citation:
PMID:  4477005     Owner:  NLM     Status:  MEDLINE    
Several esters of the alpha-N-toluene-p-sulphonyl and alpha-N-benzoyl derivatives of S-(3-aminopropyl)-l-cysteine and the methyl ester of S-(4-aminobutyl)-N-toluene-p-sulphonyl-l-cysteine were synthesized. The kinetics of hydrolysis of these and esters of the alpha-N-toluene-p-sulphonyl and alpha-N-benzoyl derivatives of l-arginine, l-lysine, S-(2-aminoethyl)-l-cysteine and esters of gamma-guanidino-l-alpha-toluene-p-sulphonamidobutyric acid and alpha-N-toluene-p-sulphonyl-l-homoarginine by alpha- and beta-trypsin were compared. On the basis of values of the specificity constants (k(cat.)/K(m)), the two enzymes display similar catalytic efficiency towards some substrates. In other cases alpha-trypsin is less efficient than beta-trypsin. It is possible that alpha-trypsin possesses greater molecular flexibility than beta-trypsin.
D V Roberts; D T Elmore
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  141     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1974 Aug 
Date Detail:
Created Date:  1975-05-27     Completed Date:  1975-05-27     Revised Date:  2010-09-10    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  545-54     Citation Subset:  IM    
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MeSH Terms
Arginine / analogs & derivatives
Cysteine / analogs & derivatives
Guanidines / analogs & derivatives
Lysine / analogs & derivatives
Structure-Activity Relationship
Tosyl Compounds
Reg. No./Substance:
0/Esters; 0/Guanidines; 0/Tosyl Compounds; 52-90-4/Cysteine; 56-87-1/Lysine; 74-79-3/Arginine; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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