Document Detail


The complete amino acid sequences of two serine proteinase inhibitors from the fruiting bodies of a basidiomycete, Pleurotus ostreatus.
MedLine Citation:
PMID:  7840656     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The complete amino acid sequences of two isomeric endogenous inhibitors, IA-1 and IA-2, both of which specifically inhibit an intracellular serine proteinase (proteinase A) purified from the fruiting bodies of a higher basidiomycete, Pleurotus ostreatus, were determined. Both inhibitors are acidic polypeptides with respective molecular masses of 8307 and 8244 Da, as determined by plasma desorption mass spectral analyses, and their N-terminal serine residue is blocked by acetylation. The fragments generated from the inhibitors by proteolytic and chemical cleavages were subjected to amino acid composition, sequence, and mass spectral analyses. The sequence and molecular mass information for the peptides established that the inhibitors both consisted of 76 amino acid residues and differed from each other in that aspartic acid and glutamic acid residues at residues 12 and 15 of IA-1 were replaced by glycine and aspartic acid in IA-2, respectively. The molecular masses of IA-1 and IA-2 were calculated to be 8309 and 8237, based on the sequence data. The action of carboxypeptidase Y on IA-1 resulted in a complete loss of the inhibitory activity along with successive release of glutamine and threonine from the C-terminus. Cyanogen bromide cleavage of Met38-Pro39 and Met41-Lys42 in IA-1 and hydroxylamine degradation of IA-2 completely abolished their inhibitory activity. These results suggest that the whole molecules of both inhibitors are essential to their inhibitory activities. Their structural resemblance to propeptides of subtilisin family proteinases revealed their mechanism of action.
Authors:
N Dohmae; K Takio; Y Tsumuraya; Y Hashimoto
Related Documents :
12387886 - A novel subtilase from common bean leaves.
24862006 - Enhanced fermentability of poplar by combination of alkaline peroxide pretreatment and ...
8541296 - Over-expression of a new photo-active halorhodopsin in halobacterium salinarium.
9028866 - Complete amino acid sequence of an acidic, cardiotoxic phospholipase a2 from the venom ...
15353346 - N-nitrosations of basic amino acid residues in polypeptide.
18507366 - Synthesis and biological evaluation of d-amino acid oxidase inhibitors.
Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  316     ISSN:  0003-9861     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  1995 Jan 
Date Detail:
Created Date:  1995-03-02     Completed Date:  1995-03-02     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:  498-506     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Faculty of Science, Saitama University, Urawa, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acids / analysis
Chromatography, High Pressure Liquid
Cyanogen Bromide
Endopeptidases / metabolism
Enzyme Inhibitors*
Fungal Proteins / chemistry*,  genetics
Mass Spectrometry
Molecular Sequence Data
Molecular Weight
Peptide Fragments / chemistry
Polyporaceae / chemistry*
Sequence Analysis
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Enzyme Inhibitors; 0/Fungal Proteins; 0/IA-1 protein, Pleurotus ostreatus; 0/IA-2 protein, Pleurotus ostreatus; 0/Peptide Fragments; 506-68-3/Cyanogen Bromide; EC 3.4.-/Endopeptidases

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


Previous Document:  Light-dependent inhibition of protein kinase C and superoxide generation of neutrophils by hypericin...
Next Document:  In vitro processing of anthrax toxin protective antigen by recombinant PC1 (SPC3) and bovine interme...