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Human alpha beta hydrolase domain containing protein 11 and its yeast homolog are lipid hydrolases.

Madhuri, A. and Malathi, Srinivasan and Ram, Rajasekharan (2017) Human alpha beta hydrolase domain containing protein 11 and its yeast homolog are lipid hydrolases. Biochemical and Biophysical Research Communications, 487 (4). pp. 875-880. ISSN 0006-291X

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Mammalian alpha/beta hydrolase domain (ABHD) family of proteins have emerged as key regulators of lipid metabolism and are found to be associated with human diseases. Human α/β-hydrolase domain containing protein 11 (ABHD11) has recently been predicted as a potential biomarker for human lung adenocarcinoma. In silico analyses of the ABHD11 protein sequence revealed the presence of a conserved lipase motif GXSXG. However, the role of ABHD11 in lipid metabolism is not known. To understand the biological function of ABHD11, we heterologously expressed the human ABHD11 in budding yeast, Saccharomyces cerevisiae. In vivo [14C]acetate labeling of cellular lipids in yeast cells overexpressing ABHD11 showed a decrease in triacylglycerol content. Overexpression of ABHD11 also alters the molecular species of triacylglycerol in yeast. Similar activity was observed in its yeast homolog, Ygr031w. The role of the conserved lipase motif in the hydrolase activity was proven by the mutation of all conserved amino acid residues of GXSXG motif. Collectively, our results demonstrate that human ABHD11 and its yeast homolog YGR031W have a pivotal role in the lipid metabolism.

Item Type: Article
Uncontrolled Keywords: ABHD11 (NM_148912); Acyl hydrolase; In vivo labeling; Triacylglycerol
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 11 Lipid Biochemistry
Divisions: Dept. of Lipid Science
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 01 Feb 2018 11:15
Last Modified: 01 Feb 2018 11:15
URI: http://ir.cftri.com/id/eprint/13396

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