期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 519, 期 2, 页码 274-279出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2019.08.166
关键词
Enterobacter asburiae; CinB; Lipase; Acetyl esterase; alpha/beta fold-hydrolase
资金
- Program for Liaoning Excellent Talents in University [LJQ2015030]
- Natural Science Foundation of Liaoning Province [2019-MS-065]
- Fundamental Research Funds for the Central Universities [DC201502020203, DC201502020201]
- National Natural Science Foundation of China [81672498]
- National Research Foundation of Korea (NRF) - Korean government (MOE) [NRF-2017R1D1A1B03033087, 2017M3A9F6029736]
- National Research Foundation of Korea [2017M3A9F6029736] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Lipases are widely present in various plants, animals and microorganisms, constituting a large category of enzymes. They have the ability to catalyze the cleavage of ester bonds. The lipase CinB from Enterobacter asburiae (E. asburiae) is an acetyl esterase. The primary amino acid sequence suggests that the EaCinB protein belongs to the alpha/beta-hydrolase (ABH) superfamily of the esterase/lipase superfamily. However, its molecular functions have not yet been determined. Here, we report the crystal structure of E. asburiae CinB at a 1.45 angstrom resolution. EaCinB contains a signal peptide, cap domain and catalytic domain. The active site of EaCinB contains the catalytic triad (Ser180-His307-Asp277) on the catalytic domain. The oxyanion hole is composed of Gly106 and Gly107 within the conserved sequence motif HGGG (amino acid residues 106-109). The substrate is accessible between the alpha 1 and alpha 2 helices or the alpha 1 helix and catalytic domain. Narrow substrate pockets are formed by the alpha 2 helix of the cap domain. Site-directed mutagenesis showed that EaCinB-W208H exhibits a higher catalytic ability than EaCinB-WT by approximately nine times. Our results provide insight into the molecular function of EaCinB. (C) 2019 Elsevier Inc. All rights reserved.
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