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Characterization and Mutation Anaylsis of a Cold-Active Bacterial Hormone-Sensitive Lipase From Salinisphaera Sp. P7-4

Characterization and Mutation Anaylsis of a Cold-Active Bacterial Hormone-Sensitive Lipase From Salinisphaera Sp. P7-4

Boo-Young Kim, Wanki Yoo, Ly Thi Huong Luu Le, Kyeong Kyu Kim, Han-Woo Kim, Jun Hyuck Lee, Young-Ok Kim, T Doohun Kim

Arch Biochem Biophys. 2019 Mar 15;663:132-142.

PMID: 30653961

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 (Leu156, Phe164, and Val204) around the substrate-binding pocket were involved in substrate recognition. In addition, highly conserved amino acids (Glu201, Arg207, Leu208, and Asp227) 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP60015	Glyceryl tributyrate		60-01-5	Price

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