Document Detail


A kinetic study of hog kidney aminoacylase.
MedLine Citation:
PMID:  7066334     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The kinetic and thermodynamic parameters of the hog kidney acylase-catalyzed reactions of N-acetyl-L-methionine hydrolysis and synthesis have been investigated. The equilibrium constants were determined at high concentrations of the products (acetate and L-amino acid) for a number of amino acids. A kinetic scheme of the enzymatic reaction was proposed that describes the dependence of the rate of hydrolytic and synthetic reactions on the composition of the reaction system. The kinetic parameters determined from the progress curves proved very close to those obtained by the initial rate analysis. The kinetic and thermodynamic constants fitted the Haldane equation.
Authors:
Galaev IYu; V K Svedas
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  701     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1982 Mar 
Date Detail:
Created Date:  1982-06-24     Completed Date:  1982-06-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  389-94     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amidohydrolases / metabolism*
Amino Acids / metabolism
Animals
Hydrogen-Ion Concentration
Hydrolysis
Kidney / enzymology*
Kinetics
Mathematics
Methionine / analogs & derivatives,  metabolism
Substrate Specificity
Swine
Thermodynamics
Chemical
Reg. No./Substance:
0/Amino Acids; 63-68-3/Methionine; 65-82-7/N-acetylmethionine; EC 3.5.-/Amidohydrolases; EC 3.5.1.14/aminoacylase I

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


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