Document Detail


An aspartic protease analogue: intermolecular catalysis of peptide hydrolysis by carboxyl groups.
MedLine Citation:
PMID:  11378379     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Two aspartic carboxyl groups act as key catalytic groups in the active site of an aspartic protease. We synthesized an aspartic protease analogue by positioning three salicylate residues in close proximity on a cross-linked polystyrene. The immobile artificial protease effectively hydrolyzed albumin into many small fragments by the catalytic action of carboxyl groups contained in the active site. The artificial protease manifested optimum activity at pH 3 just as aspartic proteases.
Authors:
S Oh; W Chang; J Suh
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Bioorganic & medicinal chemistry letters     Volume:  11     ISSN:  0960-894X     ISO Abbreviation:  Bioorg. Med. Chem. Lett.     Publication Date:  2001 Jun 
Date Detail:
Created Date:  2001-05-29     Completed Date:  2001-09-06     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9107377     Medline TA:  Bioorg Med Chem Lett     Country:  England    
Other Details:
Languages:  eng     Pagination:  1469-72     Citation Subset:  IM    
Affiliation:
School of Chemistry and Molecular Engineering and Center for Molecular Catalysis, Seoul National University, 151-747, Seoul, Republic of Korea.
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MeSH Terms
Descriptor/Qualifier:
Albumins / metabolism*
Aspartic Acid Endopeptidases / chemistry,  metabolism
Catalysis
Hydrogen-Ion Concentration
Hydrolysis
Molecular Mimicry
Peptides / metabolism
Polystyrenes / chemistry*
Salicylates / chemistry*
Chemical
Reg. No./Substance:
0/Albumins; 0/Peptides; 0/Polystyrenes; 0/Salicylates; EC 3.4.23.-/Aspartic Acid Endopeptidases

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


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