Document Detail

Specificity and inhibition studies of Armillaria mellea protease.
MedLine Citation:
PMID:  23849     Owner:  NLM     Status:  MEDLINE    
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.
W G Lewis; J M Basford; P L Walton
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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    
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MeSH Terms
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*
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; EC 3.4.-/Peptide Hydrolases

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