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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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
id crfrontiers:10.18388/abp.2015_1065
record_format openpolar
spelling crfrontiers:10.18388/abp.2015_1065 2024-09-15T17:47:31+00:00 Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica. Strzelczyk, Paweł Bujacz, Grzegorz D Kiełbasiński, Piotr Błaszczyk, Jarosław 2015 http://dx.doi.org/10.18388/abp.2015_1065 https://ojs.ptbioch.edu.pl/index.php/abp/article/download/1683/318 unknown Frontiers Media SA Acta Biochimica Polonica volume 63, issue 1 ISSN 1734-154X 0001-527X journal-article 2015 crfrontiers https://doi.org/10.18388/abp.2015_1065 2024-07-23T04:04:16Z 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. Article in Journal/Newspaper Antarc* Antarctica Frontiers (Publisher) Acta Biochimica Polonica 63 1
institution Open Polar
collection Frontiers (Publisher)
op_collection_id crfrontiers
language unknown
description 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.
format Article in Journal/Newspaper
author Strzelczyk, Paweł
Bujacz, Grzegorz D
Kiełbasiński, Piotr
Błaszczyk, Jarosław
spellingShingle Strzelczyk, Paweł
Bujacz, Grzegorz D
Kiełbasiński, Piotr
Błaszczyk, Jarosław
Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.
author_facet Strzelczyk, Paweł
Bujacz, Grzegorz D
Kiełbasiński, Piotr
Błaszczyk, Jarosław
author_sort Strzelczyk, Paweł
title Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.
title_short Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.
title_full Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.
title_fullStr Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.
title_full_unstemmed Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.
title_sort crystal and molecular structure of hexagonal form of lipase b from candida antarctica.
publisher Frontiers Media SA
publishDate 2015
url http://dx.doi.org/10.18388/abp.2015_1065
https://ojs.ptbioch.edu.pl/index.php/abp/article/download/1683/318
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Acta Biochimica Polonica
volume 63, issue 1
ISSN 1734-154X 0001-527X
op_doi https://doi.org/10.18388/abp.2015_1065
container_title Acta Biochimica Polonica
container_volume 63
container_issue 1
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