Document Detail


Enzyme-substrate interactions in the hydrolysis of peptide substrates by thermitase, subtilisin BPN', and proteinase K.
MedLine Citation:
PMID:  3511847     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Peptide substrates of the general structure acetyl-Alan (n = 2-5), acetyl-Pro-Ala-Pro-Phe-Alan-NH2 (n = 0-3), and acetyl-Pro-Ala-Pro-Phe-AA-NH2 (AA = various amino acids) were synthesized and used to investigate the enzyme-substrate interactions of the microbial serine proteases thermitase, subtilisin BPN', and proteinase K on the C-terminal side of the scissile bond. The elongation of the substrate peptide chain up to the second amino acid on the C-terminal side (P'2) enhances the hydrolysis rate of thermitase and subtilisin BPN', whereas for proteinase K an additional interaction with the third amino acid (P'3) is possible. The enzyme subsite S'1 specificity of the proteases investigated is very similar. With respect to kcat/Km values small amino acid residues such as Ala and Gly are favored in this position. Bulky residues such as Phe and Leu were hydrolyzed to a lower extent. Proline in P'1 abolishes the hydrolysis of the substrates. Enzyme-substrate interactions on the C-terminal side of the scissile bond appear to affect kcat more than Km for all three enzymes.
Authors:
D Brömme; K Peters; S Fink; S Fittkau
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  244     ISSN:  0003-9861     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  1986 Feb 
Date Detail:
Created Date:  1986-03-13     Completed Date:  1986-03-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  439-46     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Chymotrypsin / pharmacology
Endopeptidase K
Endopeptidases / pharmacology*
Hydrolysis
Kinetics
Peptides*
Protein Conformation
Serine Endopeptidases*
Structure-Activity Relationship
Substrate Specificity
Subtilisins / pharmacology*
Chemical
Reg. No./Substance:
0/Peptides; EC 3.4.-/Endopeptidases; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.-/Subtilisins; EC 3.4.21.-/thermitase; EC 3.4.21.1/Chymotrypsin; EC 3.4.21.64/Endopeptidase K

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


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