Document Detail


Lipases catalyse hydrolysis of fatty acid anhydrides.
MedLine Citation:
PMID:  2226444     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Regio-specific and non-regio-specific lipases from mammals and microorganisms catalyse the hydrolysis of short, medium and long-chain fatty acid anhydrides. All the lipases tested in the present study can catalyse the hydrolysis of pure fatty acid anhydrides more efficiently than that of glycerol tributyrate. Molecular turnovers more than four times higher than that measured using glycerol tributyrate were calculated. The presence of 0.5% (by mass) anhydride in a triacylglyceride can double the initial rate of proton release during enzymatic hydrolysis. This should be taken into account when testing the chain specificity of a lipase for various synthetic substrates. Lipase inhibition was found to be associated very often with anhydride hydrolysis. The inhibition rates depended on the anhydride and the origin of the lipase. Inhibition of lipase activity is probably due to the formation of a poorly reversible acyl-lipase complex which differs from the classical fully reversible acyl-lipase complex at the catalytic centre.
Authors:
G Pieroni; J D Fourneron
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Publication Detail:
Type:  In Vitro; Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  193     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1990 Oct 
Date Detail:
Created Date:  1990-12-14     Completed Date:  1990-12-14     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  249-53     Citation Subset:  IM    
Affiliation:
Centre de Biochimie et de Biologie Moléculaire, Centre National de la Recherche Scientifique, Marseille, France.
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MeSH Terms
Descriptor/Qualifier:
Anhydrides / metabolism*
Animals
Candida / enzymology
Dogs
Fatty Acids / chemistry
Hydrogen-Ion Concentration
Kinetics
Lipase / metabolism*
Pancreas / enzymology
Pseudomonas / enzymology
Rhizopus / enzymology
Structure-Activity Relationship
Substrate Specificity
Swine
Chemical
Reg. No./Substance:
0/Anhydrides; 0/Fatty Acids; EC 3.1.1.3/Lipase

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


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