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

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...

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Bibliographic Details
Published in:Acta Biochimica Polonica
Main Authors: Strzelczyk, Paweł, Bujacz, Grzegorz D, Kiełbasiński, Piotr, Błaszczyk, Jarosław
Format: Article in Journal/Newspaper
Language:unknown
Published: Frontiers Media SA 2015
Subjects:
Antarc*
Antarctica
Online Access:http://dx.doi.org/10.18388/abp.2015_1065
https://ojs.ptbioch.edu.pl/index.php/abp/article/download/1683/318
Description
Summary: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.

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