3FAK
Structural and Functional Analysis of a Hormone-Sensitive Lipase like EstE5 from a Metagenome Library
Summary for 3FAK
| Entry DOI | 10.2210/pdb3fak/pdb |
| Descriptor | Esterase/lipase, CHLORIDE ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | hsl, este5, esterase, lipase, hydrolase |
| Biological source | uncultured bacterium |
| Total number of polymer chains | 1 |
| Total formula weight | 34706.37 |
| Authors | Hwang, K.Y.,Nam, K.H. (deposition date: 2008-11-17, release date: 2009-02-10, Last modification date: 2023-11-01) |
| Primary citation | Nam, K.H.,Kim, M.-Y.,Kim, S.-J.,Priyadarshi, A.,Lee, W.H.,Hwang, K.Y. Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase Biochem.Biophys.Res.Commun., 379:553-556, 2009 Cited by PubMed 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. PubMed: 19116143DOI: 10.1016/j.bbrc.2008.12.085 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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