Abstract
Hormone-sensitive lipase (HSL) plays an important role in the regulation of rodent fat cell lipolysis. It is regarded as an adipose tissue-specific enzyme whose sole metabolic role is the catalysis of hormone-stimulated lipolysis in mammalian cells. In this report we describe the functional and structural analysis of an EstE5 protein from a soil metagenome library. Function analysis results indicated that EstE5 preferentially hydrolyzes short-chain ester compounds, and our kinetic studies revealed the optimal pH and temperature. Based on the structural analysis, we defined the active site and the binding pocket. Structurally, EstE5 belongs to the HSL family and these structural studies may have applications in the production of value-added products, including pharmaceuticals.
Original language | English |
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Pages (from-to) | 553-556 |
Number of pages | 4 |
Journal | Biochemical and biophysical research communications |
Volume | 379 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2009 Feb 6 |
Keywords
- Crystal structure
- EstE5
- Esterase/lipase
- HSL family
- Hormone-sensitive lipase
- Soil metagenome library
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology