Characterization and mutation anaylsis of a cold-active bacterial hormone-sensitive lipase from Salinisphaera sp. P7-4
- Authors
- Kim, Boo-young; Yoo, Wanki; Le, Ly Thi Huong Luu; Kim, Kyeong Kyu; Kim, Han-Woo; Lee, Jun Hyuck; Kim, Young-Ok; Kim, T. Doohun
- Issue Date
- Mar-2019
- Publisher
- ELSEVIER SCIENCE INC
- Keywords
- SaHSL; Hormone-sensitive lipase; Salinisphaera sp. P7-4
- Citation
- ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, v.663, pp 132 - 142
- Pages
- 11
- Journal Title
- ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
- Volume
- 663
- Start Page
- 132
- End Page
- 142
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/3764
- DOI
- 10.1016/j.abb.2019.01.010
- ISSN
- 0003-9861
1096-0384
- Abstract
- In mammals, hormone sensitive lipase (EC 3.1.1.79, HSL) catalyzes the hydrolysis of triacylglycerols as well as the modifications of a broad range of hydrophobic substrates containing ester linkages. HSLs are composed of an N-terminal ligand-binding domain and a C-terminal catalytic domain. Bacterial hormone-sensitive lipases (bHSLs), which are homologous to the C-terminal domain of mammalian HSLs, have a catalytic triad composed of Ser, His, and Asp. Here, a novel cold-active hormone-sensitive lipase (SaHSL) from Salinisphaera sp. P7-4 was identified, functionally characterized, and subjected to site-directed mutations. The enzymatic properties of SaHSL were investigated using several biochemical and biophysical methods. Interestingly, SaHSL exhibited the ability to act on a broad range of substrates including glyceryl tributyrate and glucose pentaacetate. Homology modeling and site-directed mutagenesis indicated that hydrophobic residues (Leu(156), Phe(164), and Val(204)) around the substrate-binding pocket were involved in substrate recognition. In addition, highly conserved amino acids (Glu(201), Arg(207), Leu(208), and Asp(227)) in the regulatory regions were found to be responsible for substrate specificity, thermostability, and enantioselectivity. In summary, this work provides new insights into the understanding of the C-terminal domain of HSL family and evidence that SaHSL can be used in a wide range of industrial applications.
- Files in This Item
-
Go to Link
- Appears in
Collections - 이과대학 > 화학과 > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.