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

被引：16

作者：

Strzelczyk, Pawel ^{[1
]}

Bujacz, Grzegorz D. ^{[1
]}

Kielbasinski, Piotr ^{[2
]}

Blaszczyk, Jaroslaw ^{[2
]}

机构：

[1] Lodz Univ Technol, Inst Tech Biochem, Lodz, Poland

[2] Polish Acad Sci, Ctr Mol & Macromol Studies, Dept Heteroorgan Chem, Lodz, Poland

来源：

ACTA BIOCHIMICA POLONICA | 2016年 / 63卷 / 01期

关键词：

CAL-B; lipase B; Candida antarctica; apo form; crystallographic polymorphism; macromolecular crystallography; DYNAMIC KINETIC RESOLUTION; CATALYZED SYNTHESIS; PROMISCUITY; ALCOHOLYSIS; HYDROLYSIS; REFINEMENT; INSIGHTS; SITE;

D O I：

10.18388/abp.2015_1065

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：103 / 109

页数：7

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