Document Detail


Stereospecificity of amino acid hydroxamate inhibition of aminopeptidases.
MedLine Citation:
PMID:  6643439     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Hydroxamates of amino acids and aliphatic acids are effective inhibitors of Aeromonas proteolytica amino-peptidase (EC 3.4.11.10) and of both the cytosolic (EC 3.4.11.1) and microsomal (EC 3.4.11.2) aminopeptidases of swine kidney. Cytosolic leucine aminopeptidase and the Aeromonas enzyme were inhibited to a greater extent by D isomers than by the L enantiomorphs, manganese-activated kidney cytosolic leucine aminopeptidase being inhibited 10 times more effectively by D-leucine and D-valine hydroxamic acids than by the L isomers. The D isomers of these two compounds inhibited Aeromonas aminopeptidase to an even greater extent with Ki values of 2 X 10(-9) and 5 X 10(-9), respectively, whereas the corresponding L isomers were bound 150 times less tightly. With the Aeromonas enzyme, a comparison of inhibition by racemic mixtures with that of the corresponding L isomers indicated that in all cases the contribution of the D isomer was predominant. Isocaproic hydroxamic acid inhibited this enzyme equally well as L-leucine hydroxamic acid, indicating that the amino group orientation in the D isomer contributes to the binding efficacy. Swine kidney microsomal aminopeptidase was also inhibited by D isomers of leucine and valine hydroxamic acids but in contrast to the other two enzymes, the inhibition was 10-fold less than that observed for the corresponding L isomers. Cytosolic leucine aminopeptidase with either 6 g atoms of zinc per mol or 12 g atoms of zinc per mol was inhibited only slightly by any of the hydroxamic acid compounds; evidently enzyme-bound manganese (or magnesium) is specific for hydroxamate binding to this aminopeptidase.
Authors:
S H Wilkes; J M Prescott
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  258     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1983 Nov 
Date Detail:
Created Date:  1984-01-07     Completed Date:  1984-01-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  13517-21     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Aeromonas / enzymology*
Amino Acids / pharmacology*
Animals
Cytosol / enzymology
Hydroxamic Acids / pharmacology*
Kidney / enzymology*
Kinetics
Leucyl Aminopeptidase / antagonists & inhibitors*
Microsomes / enzymology*
Structure-Activity Relationship
Swine
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Hydroxamic Acids; EC 3.4.11.1/Leucyl Aminopeptidase

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


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