한빛사논문
- 조회2,996
Abstract
Tri Duc Ngo,a‡ Bum Han Ryu,b‡ Hansol Ju,b Eunjin Jang,b Kwangsoo Park,a Kyeong Kyu Kima* and T. Doohun Kimb*
aDepartment of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Republic of Korea, and
bDepartment of Molecular Science and Technology, Graduate School of Interdisciplinary Programs, Ajou University, Suwon 443-749, Republic of Korea
‡ These authors contributed equally to this work.
* Correspondence
Abstract
Intracellular mobilization of fatty acids from triacylglycerols in mammalian adipose tissues proceeds through a series of lipolytic reactions. Among the enzymes involved, hormone-sensitive lipase (HSL) is noteworthy for its central role in energy homeostasis and the pathogenic role played by its dysregulation. By virtue of its broad substrate specificity, HSL may also serve as an industrial biocatalyst. In a previous report, Est25, a bacterial homologue of HSL, was identified from a metagenomic library by functional screening. Here, the crystal structure of Est25 is reported at 1.49Å resolution; it exhibits an α/β-hydrolase fold consisting of a central β-sheet enclosed by α-helices on both sides. The structural features of the cap domain, the substrate-binding pocket and the dimeric interface of Est25, together with biochemical and biophysical studies including native PAGE, mass spectrometry, dynamic light scattering, gel filtration and enzyme assays, could provide a basis for understanding the properties and regulation of hormone-sensitive lipase (HSL). The increased stability of cross-linked Est25 aggregates (CLEA-Est25) and their potential for extensive reuse support the application of this preparation as a biocatalyst in biotransformation processes.
PDB reference: 4j7a
Keywords: Est25; hormone-sensitive lipase.
논문정보
- Research article
- 2013년 08월 (BRIC 등록일 2013-08-20)
- 국내 연구진
- 의약학 > 분자세포의학
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