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Sequence-specific apolipoprotein A-I effects on lecithin:cholesterol acyltransferase activity.

Abstract：

:Existing kinetic data of cholesteryl ester formation by lecithin:cholesterol acyltransferase in discoidal high-density lipoproteins with 34 mutations of apoA-I that involved all putative helices were grouped by cluster analysis into four noncoincident regions with mutations both without any functional impairment and with profound isolated (V- and K-mutations) or common (VK-mutations) effect on V(max)(app) and K(m)(app). Data were analyzed with a new kinetic model of LCAT activity at interface that exploits the efficiency of LCAT binding to the particle, particle dimensions, and surface concentrations of phosphatidylcholine and cholesterol. V-mutations with major location in the central part and C-domain affected the second-order rate constant of cholesteryl ester formation at the solvolysis of acyl-enzyme intermediate by cholesterol as nucleophile. The central region in apoA-I sequence is suggested to influence the proper positioning of cholesterol molecule toward LCAT active center with major contribution of arginine residue(s). K-mutations with major location in N-domain may affect binding and stability of enzyme-phosphatidylcholine complex. VK-mutations may possess mixed effects; the independent binding measurement may segregate individual steps.

journal_name

Mol Cell Biochem

journal_title

Molecular and cellular biochemistry

authors

Dergunov AD

doi

10.1007/s11010-013-1619-5

subject

Has Abstract

pub_date

2013-06-01 00:00:00

pages

283-90

issue

1-2

eissn

0300-8177

issn

1573-4919

journal_volume

378

pub_type

杂志文章

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