3FAK

Structural and Functional Analysis of a Hormone-Sensitive Lipase like EstE5 from a Metagenome Library

3FAK の概要

• エントリーDOI: 10.2210/pdb3fak/pdb
• 分子名称: Esterase/lipase, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: hsl, este5, esterase, lipase, hydrolase
• 由来する生物種: uncultured bacterium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34706.37

構造登録者

Hwang, K.Y.,Nam, K.H. (登録日: 2008-11-17, 公開日: 2009-02-10, 最終更新日: 2023-11-01)

主引用文献

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

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: 19116143
DOI: 10.1016/j.bbrc.2008.12.085

実験手法

X-RAY DIFFRACTION (1.9 Å)