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    
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.
D Brömme; K Peters; S Fink; S Fittkau
Related Documents :
25262797 - A review on parp1 inhibitors: pharmacophore modeling, virtual and biological screening ...
18937627 - Biochemical characterization of the catalytic domains of three different clostridial co...
10074467 - Mutational analysis of active-site residues of the enterococcal d-ala-d-ala dipeptidase...
25486447 - Structure guided lead generation for m. tuberculosis thymidylate kinase (mtb tmk): disc...
2738877 - Bifunctional antitumor compounds: synthesis and characterization of a au(iii)-streptoni...
10506917 - Sodium transport systems in human chondrocytes. i. morphological and functional express...
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    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Chymotrypsin / pharmacology
Endopeptidase K
Endopeptidases / pharmacology*
Protein Conformation
Serine Endopeptidases*
Structure-Activity Relationship
Substrate Specificity
Subtilisins / pharmacology*
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; EC K

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

Previous Document:  Deoxyribonucleotide biosynthesis in yeast: assay and properties of ribonucleotide reductase in perme...
Next Document:  Differential sensitivities of the subunits of mammalian ribonucleotide reductase to proteases, sulfh...