Document Detail


Specificity and inhibition studies of Armillaria mellea protease.
MedLine Citation:
PMID:  23849     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The action of Armillaria mellea protease has been evaluated on a number of polypeptide substrates. It has been shown to split the Pro7-Lys8 bonds in both native and oxidised lysine-vasopressin and the Ser11-Lys12 bond in glucagon. No other splits were detected in these substrates. The enzyme also caused extensive degradation of S-carboxymethyl lysozyme, S-carcoxymethyl pepsinogen and oxidised ribonuclease. A. In each case the only new amino-terminal residue to appear was lysine. A. mellea protease was inhibited by the chelating agents 1,10-phenanthroline, alpha, alpha'-bipyridine and imidazole. The pK1 values (negative log10 of concentration required for 50% inhibition) for these three inhibitors were 3.9, 3.4 and 1.1, respectively. Lysine, S-2-aminoethylcysteine and short chain aliphatic amines also proved to be relatively good inhibitors of A. mellea protease while arginine was a poor inhibitor.
Authors:
W G Lewis; J M Basford; P L Walton
Related Documents :
3020549 - Endogenous inhibitor of nonlysosomal high molecular weight protease and calcium-depende...
17194619 - Proteomic discovery of protease substrates.
10779309 - Trypsin-like protease of mites: purification and characterization of trypsin-like prote...
20799349 - A lead discovery strategy driven by a comprehensive analysis of proteases in the peptid...
11378379 - An aspartic protease analogue: intermolecular catalysis of peptide hydrolysis by carbox...
20158239 - Botulinum neurotoxin a protease: discovery of natural product exosite inhibitors.
25478849 - The structure of vanin 1: a key enzyme linking metabolic disease and inflammation.
18313309 - Degradation-promoters of cellular inhibitor of apoptosis protein 1 based on bestatin an...
11722579 - Identification of molecular determinants required for interaction of ubiquitin-conjugat...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  522     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1978 Feb 
Date Detail:
Created Date:  1978-04-17     Completed Date:  1978-04-17     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  551-60     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amines / pharmacology
Amino Acids / analysis
Basidiomycota / enzymology*
Chelating Agents / pharmacology
Glucagon / metabolism
Hydrogen-Ion Concentration
Lypressin / metabolism
Lysine / pharmacology
Muramidase / metabolism
Pepsinogens / metabolism
Peptide Hydrolases / isolation & purification,  metabolism*
Chemical
Reg. No./Substance:
0/Amines; 0/Amino Acids; 0/Chelating Agents; 0/Pepsinogens; 50-57-7/Lypressin; 56-87-1/Lysine; 9007-92-5/Glucagon; EC 3.2.1.17/Muramidase; EC 3.4.-/Peptide Hydrolases

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


Previous Document:  Acid glycohydrolase in Chinese hamster with spontaneous diabetes. I. Depressed levels of renal alpha...
Next Document:  Purification and partial characterization of rat brain acid proteinase (isorenin).