Document Detail


Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases.
MedLine Citation:
PMID:  16325466     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We have studied the kinetics of hydrolysis of triacylglycerols, vinyl esters and p-nitrophenyl butyrate by four carboxylesterases of the HSL family, namely recombinant human hormone-sensitive lipase (HSL), EST2 from Alicyclobacillus acidocaldarius, AFEST from Archeoglobus fulgidus, and protein RV1399C from Mycobacterium tuberculosis. The kinetic properties of enzymes of the HSL family have been compared to those of a series of lipolytic and non-lipolytic carboxylesterases including human pancreatic lipase, guinea pig pancreatic lipase related protein 2, lipases from Mucor miehei and Thermomyces lanuginosus, cutinase from Fusarium solani, LipA from Bacillus subtilis, porcine liver esterase and Esterase A from Aspergilus niger. Results indicate that human HSL, together with other lipolytic carboxylesterases, are active on short chain esters and hydrolyze water insoluble trioctanoin, vinyl laurate and olive oil, whereas the action of EST2, AFEST, protein RV1399C and non-lipolytic carboxylesterases is restricted to solutions of short chain substrates. Lipolytic and non-lipolytic carboxylesterases can be differentiated by their respective value of K(0.5) (apparent K(m)) for the hydrolysis of short chain esters. Among lipolytic enzymes, those possessing a lid domain display higher activity on tributyrin, trioctanoin and olive oil suggesting, then, that the lid structure contributes to enzyme binding to triacylglycerols. Progress reaction curves of the hydrolysis of p-nitrophenyl butyrate by lipolytic carboxylesterases with lid domain show a latency phase which is not observed with human HSL, non-lipolytic carboxylesterases, and lipolytic enzymes devoid of a lid structure as cutinase.
Authors:
Henri Chahinian; Yassine Ben Ali; Abdelkarim Abousalham; Stefan Petry; Luigi Mandrich; Guiseppe Manco; Stephane Canaan; Louis Sarda
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Publication Detail:
Type:  Comparative Study; Journal Article     Date:  2005-11-17
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1738     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2005 Dec 
Date Detail:
Created Date:  2006-01-27     Completed Date:  2006-03-17     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  29-36     Citation Subset:  IM    
Affiliation:
Laboratoire d'Enzymologie Interfaciale et de Physiologie de la lipolyse, UPR9025-CNRS, 31 Chemin J. Aiguier, 13402 Marseille Cedex 20, France. chahin@ibsm.cnrs-mrs.fr
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / genetics,  metabolism
Butyrates / metabolism
Carboxylic Ester Hydrolases / genetics,  metabolism*
Humans
Hydrogen-Ion Concentration
Hydrolysis
Kinetics
Lipase / metabolism
Molecular Sequence Data
Octanoic Acids / metabolism
Plant Oils / metabolism
Recombinant Proteins / metabolism
Sequence Homology, Amino Acid
Sterol Esterase / metabolism*
Substrate Specificity
Triglycerides / metabolism
Vinyl Compounds / metabolism
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Butyrates; 0/LipA protein, Bacteria; 0/Octanoic Acids; 0/Plant Oils; 0/Recombinant Proteins; 0/Triglycerides; 0/Vinyl Compounds; 123-20-6/vinyl butyrate; 2635-84-9/4-nitrophenyl butyrate; 538-23-8/tricaprylin; 60-01-5/tributyrin; 8001-25-0/olive oil; EC 3.1.1.-/Carboxylic Ester Hydrolases; EC 3.1.1.-/Rv1399c protein, M tuberculosis; EC 3.1.1.-/cutinase; EC 3.1.1.-/pancreatic lipase related protein 2; EC 3.1.1.13/Sterol Esterase; EC 3.1.1.3/Lipase

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