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

doi:10.1016/j.bbrc.2008.12.085

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

Department of Biosystems and Biotechnology

Research output: Contribution to journal › Article › peer-review

31 Citations (Scopus)

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
Pages (from-to)	553-556
Number of pages	4
Journal	Biochemical and biophysical research communications
Volume	379
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2008.12.085
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

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10.1016/j.bbrc.2008.12.085

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Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase. / Nam, Ki Hyun; Kim, Min Young; Kim, Soo Jin; Priyadarshi, Amit; Lee, Won Ho; Hwang, Kwang Yeon.

In: Biochemical and biophysical research communications, Vol. 379, No. 2, 06.02.2009, p. 553-556.

Research output: Contribution to journal › Article › peer-review

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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.",

keywords = "Crystal structure, EstE5, Esterase/lipase, HSL family, Hormone-sensitive lipase, Soil metagenome library",

author = "Nam, {Ki Hyun} and Kim, {Min Young} and Kim, {Soo Jin} and Amit Priyadarshi and Lee, {Won Ho} and Hwang, {Kwang Yeon}",

note = "Funding Information: We thank S.Y. Park, Y.H. Yoon and F. Kawai at Yokohama City University for assistance during data collection at beamline 17A of the Photon Factory, Japan. We thank H.S. Lee, K.H. Kim, and K.J. Kim for assistance during data collection at beamline 6B of Pohang Light Source, Korea. Functional Proteomics Center, 21C Frontier Program, of the Korea Ministry of Science and Technology (M108KM010031-08K1301-03111) and the National Institute of Agricultural Biotechnology (05-4-11-16-3). K.H. Nam is supported by Brain Korea 21 project. ",

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AU - Hwang, Kwang Yeon

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PY - 2009/2/6

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N2 - 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.

AB - 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.

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

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