Nam_2009_Biochem.Biophys.Res.Commun_379_553

Reference

Title : Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase - Nam_2009_Biochem.Biophys.Res.Commun_379_553
Author(s) : Nam KH , Kim MY , Kim SJ , Priyadarshi A , Lee WH , Hwang KY
Ref : Biochemical & Biophysical Research Communications , 379 :553 , 2009
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.

PubMedSearch : Nam_2009_Biochem.Biophys.Res.Commun_379_553
PubMedID: 19116143
Gene_locus related to this paper: 9bact-Q0GMU2

Related information

Gene_locus 9bact-Q0GMU2
Structure 9bact-Q0GMU2    3FAK

Citations formats

Nam KH, Kim MY, Kim SJ, Priyadarshi A, Lee WH, Hwang KY (2009)
Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase
Biochemical & Biophysical Research Communications 379 :553

Nam KH, Kim MY, Kim SJ, Priyadarshi A, Lee WH, Hwang KY (2009)
Biochemical & Biophysical Research Communications 379 :553