Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase

Ki Hyun Nam, Min Young Kim, Soo Jin Kim, Amit Priyadarshi, Won Ho Lee, Kwang Yeon Hwang

Research output: Contribution to journalArticle

28 Citations (Scopus)


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 languageEnglish
Pages (from-to)553-556
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 2009 Feb 6



  • Crystal structure
  • EstE5
  • Esterase/lipase
  • Hormone-sensitive lipase
  • HSL family
  • Soil metagenome library

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

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