Distinction Between Esterases and Lipases: Comparative Biochemical Properties of Sequence-Related Carboxylesterases

被引:88
作者
Chahinian, H. [1 ]
Sarda, L. [2 ]
机构
[1] Univ Paul Cezanne, Fac St Jerome, Lab Biochim & Physicochim Membranes, Marseille, France
[2] Univ Aix Marseille 1, Fac St Charles, Biochim Lab, Marseille, France
关键词
HORMONE-SENSITIVE LIPASE; HUMAN PANCREATIC LIPASE; SALT ACTIVATED LIPASE; SOLANI-PISI CUTINASE; LECITHIN-CHOLESTEROL ACYLTRANSFERASE; CRYSTAL-STRUCTURE; INTERFACIAL ACTIVATION; SUBSTRATE-SPECIFICITY; KINETIC-PROPERTIES; OPEN CONFORMATION;
D O I
10.2174/092986609789071333
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Carboxylesterases (Carboxyl ester hydrolase) include two groups of enzymes, namely non-specific esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3) which have been early differentiated on the basis of their substrate specificity. Esterases hydrolyse solutions of water-soluble short acyl chain esters and are inactive against water-insoluble long chain triacylglycerols which, in turn, are specifically hydrolyzed by lipases. Based on the comparison of the primary structures, three families of sequence-related carboxylesterases, namely the lipoprotein lipase family (L-family), the hormone-sensitive lipase family (H-family) and the cholinesterase family (C-family) have been identified. Using solutions and emulsions of vinyl, glyceryl and p-nitrophenyl esters, we have reinvestigated the kinetic properties of some esterases and lipases of the H-and C-families. Results indicate that esterases and lipases, which are both active on soluble esters, can be differentiated by their value of Km. Moreover, esterase, unlike lipases, are inactive against water-insoluble esters as vinyl laurate and trioctanoylglycerol. From the the comparison of structural features of sequence-related esterases and lipases, it appears that lipases, unlike esterases, display a significant difference in the distribution of hydrophobic amino acid residues at vicinity of their active site. This observation supports the hypothesis of the existence in lipases of a particular surface domain that specifically interacts with lipid-water interfaces and contributes to the transfer a single substrate molecule from the organized lipid-water interface (supersubstrate) to the catalytic site of the enzyme.
引用
收藏
页码:1149 / 1161
页数:13
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