Abstract
The esterase Est8 from the thermophilic bacterium Bacillus sp. K91 belongs to the GDSL family and is active on a variety of acetylated compounds, including 7-aminocephalosporanic acid. In contrast to other esterases of the GDSL family, the catalytic residues Asp182 and His185 were more pivotal for the catalytic activity of Est8 than the Ser11 residue. To better understand the biochemical and enzymatic properties of Est8, recombinant Est8 protein was purified and crystallized. Crystals of Est8 were obtained by the hanging-drop vapour-diffusion method using 2.0 M ammonium sulfate, 5%(v/v) 2-propanol as the crystallization solution. X-ray diffraction data were collected to a resolution of 2.30 Å with an Rmerge of 16.4% from a crystal belonging to space group P41212 or P43212, with unit-cell parameters a = b = 68.50, c = 79.57 Å.
Highlights
The esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3) are collectively known as lipolytic enzymes, and have important physiological and biotechnological roles in the synthesis or hydrolysis of ester-containing compounds (Rubin, 1994)
Lipolytic enzymes exist in various species, the most widely exploited enzymes are produced by microorganisms (Bornscheuer, 2002)
Data sets were collected on beamline BL17U1 at the Shanghai Synchrotron Radiation Facility (SSRF), People’s Republic of China using an ADSC Q315 CCD system (Wang et al, 2015)
Summary
The esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3) are collectively known as lipolytic enzymes, and have important physiological and biotechnological roles in the synthesis or hydrolysis of ester-containing compounds (Rubin, 1994). Thermostable lipolytic enzymes are always in great demand because most industrial lipolytic hydrolase and esterification reactions take place under harsh conditions such as at high temperature or under organic solvent conditions. They are better suited to the harsh processes involved in industrial and biotechnological applications (Hess et al, 2008; Hotta et al, 2002). Est might be of significant industrial interest and value in scientific research as a thermostable esterase, and exhibits maximum activity in an alkaline environment. To provide new insights into the structure–function relationship of Est and to obtain a better understanding of the biochemical data, determination of the crystal structure of the enzyme is in progress
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