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3fak

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

Structural highlights

3fak is a 1 chain structure with sequence from Uncultured bacterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q0GMU2_9BACT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase.,Nam KH, Kim MY, Kim SJ, Priyadarshi A, Lee WH, Hwang KY Biochem Biophys Res Commun. 2009 Feb 6;379(2):553-6. Epub 2008 Dec 29. PMID:19116143^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nam KH, Kim MY, Kim SJ, Priyadarshi A, Lee WH, Hwang KY. Structural and functional analysis of a novel EstE5 belonging to the subfamily of hormone-sensitive lipase. Biochem Biophys Res Commun. 2009 Feb 6;379(2):553-6. Epub 2008 Dec 29. PMID:19116143 doi:http://dx.doi.org/10.1016/j.bbrc.2008.12.085