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

• Authors: Paweł Strzelczyk , Grzegorz Bujacz , Piotr Kiełbasiński , Jarosław Błaszczyk
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

CAL-B; lipase B; Candida antarctica; apo form; crystallographic polymorphism; macromolecular crystallography

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2016
• Volume: 63
• Issue: 1
• Pages: 103-109

Dates

published

2016

received

2015-05-21

revised

2015-10-07

accepted

2015-11-18

(unknown)

2015-12-30

Contributors

author

Paweł Strzelczyk

• Lodz University of Technology, Institute of Technical Biochemistry, Łódź, Poland

author

Grzegorz Bujacz

• Lodz University of Technology, Institute of Technical Biochemistry, Łódź, Poland

author

Piotr Kiełbasiński

• Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Department of Heteroorganic Chemistry, Łódź, Poland

author

Jarosław Błaszczyk

• Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences, Department of Heteroorganic Chemistry, Łódź, Poland

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Identifiers

DOI

10.18388/abp.2015_1065