Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.

Paweł Strzelczyk; Grzegorz D Bujacz; Piotr Kiełbasiński; Jarosław Błaszczyk

doi:10.18388/abp.2015_1065

Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.

Paweł Strzelczyk Lodz University of Technology, Institute of Technical Biochemistry, Łódź, Poland.;
Grzegorz D Bujacz Lodz University of Technology, Institute of Technical Biochemistry, Łódź, Poland.;
Piotr Kiełbasiński Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Department of Heteroorganic Chemistry, Łódź, Poland.;
Jarosław Błaszczyk Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Department of Heteroorganic Chemistry, Łódź, Poland.;

DOI: https://doi.org/10.18388/abp.2015_1065

Abstract

During crystallization screenings of commercially available hydrolytic enzymes, the new, hexagonal crystal form of CAL-B, has been discovered and hereby reported. The NAG molecules, which were closing the glycosylation site in the orthorhombic form, in hexagonal structure make the glycosylation site open. It is unknown whether the opening and closing of the glycosylation site by the 'lid' NAG molecules, could be related to the opening and closing of the active center of the enzyme upon substrate binding and product release.

Published

2015-12-30

Issue

Vol. 63 No. 1 (2016)

Section

Articles

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