Document Detail


L-usnate-urease interactions: binding sites for polymerization.
MedLine Citation:
PMID:  6223456     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
L-usnic acid inactivates urease through a process which implicates the blockade of--SH groups in parallel to the formation of inactive polymers. Both L-alanine and L-proline partially reverses the inactivation and effectively diminishes the amount of highly polymerized protein. The amino acids also prevent the linkage of L-usnic acid on the sites of low affinity for the ligand, being then related to the sites of polymerization.
Authors:
B Cifuentes; I García; C Vicente
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Zeitschrift für Naturforschung. Section C: Biosciences     Volume:  38     ISSN:  0341-0382     ISO Abbreviation:  Z. Naturforsch., C, Biosci.     Publication Date:    1983 Mar-Apr
Date Detail:
Created Date:  1983-08-11     Completed Date:  1983-08-11     Revised Date:  2009-06-08    
Medline Journal Info:
Nlm Unique ID:  7801143     Medline TA:  Z Naturforsch C     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  273-6     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Alanine / pharmacology
Benzofurans*
Kinetics
Proline / pharmacology
Protein Binding
Urease / metabolism*
Chemical
Reg. No./Substance:
0/Benzofurans; 147-85-3/Proline; 56-41-7/Alanine; EC 3.5.1.5/Urease

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


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