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Evidence for a multi-domain structure for hormone-sensitive lipase

G M Smith¹, A J Garton, A Aitken

¹Department of Biochemistry and Genetics, Medical School, University of Newcastle, Newcastle upon Tyne, UK.

|October 28, 1996

Summary

Hormone-sensitive lipase (HSL) has distinct domains for lipid and water-soluble substrates. Phosphorylation alters HSL

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Area of Science:

Biochemistry
Enzymology
Molecular Biology

Background:

Hormone-sensitive lipase (HSL) is a key enzyme in lipid metabolism.
Understanding HSL's structure-function relationship is crucial for metabolic research.

Purpose of the Study:

To investigate the domain structure of HSL.
To differentiate the catalytic domains responsible for hydrolyzing lipid versus water-soluble substrates.

Main Methods:

Limited tryptic digestion of HSL.
Active site labeling with [3H]di-isopropylfluorophosphate and [14C]orlistat.
Analysis of molecular mass of digested fragments using SDS-PAGE.

Main Results:

Tryptic digestion selectively inactivated lipid hydrolysis but not hydrolysis of p-nitrophenyl butyrate.

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A 17.6 kDa radiolabeled domain was identified, capable of hydrolyzing water-soluble substrates.

Phosphorylation of HSL followed by tryptic digestion yielded an 11.5 kDa domain.

Conclusions:

HSL possesses distinct domains for different substrate specificities.
Phosphorylation influences the domain structure and potentially the activity of HSL.
A model for HSL domain organization is proposed based on experimental evidence.