Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241.

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Population

Human embryonic kidney-293 cells expressing mutant human lipoprotein lipase (LPL)

Comparison

Site-directed mutagenesis of proposed catalytic… vs Mutation of other conserved residues

Design

Preclinical

Authors

Discussion

Confirms catalytic triad in LPL models; leaves open in vivo or therapeutic relevance for dyslipidemia.

Population

Human embryonic kidney-293 cells expressing mutant human lipoprotein lipase (LPL)

Intervention

Site-directed mutagenesis of proposed catalytic residues Ser-132, Asp-156, and His-241

Comparator

Mutation of other conserved residues (Ser-97, Ser-307, Asp-78, Asp-371, Asp-440, His-93, and His-439)

Outcome

Triolein and tributyrin esterase activities, heparin affinity, and lipid binding propertiessurrogate

Ser-132, Asp-156, and His-241 form the catalytic triad of human lipoprotein lipase and are essential for its hydrolytic activity.

Emmerich et al. (1992) studied this question.

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