Literature DB >> 26716135

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

Paweł Strzelczyk1, Grzegorz D Bujacz1, Piotr Kiełbasiński2, Jarosław Błaszczyk2.   

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.

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Year:  2015        PMID: 26716135     DOI: 10.18388/abp.2015_1065

Source DB:  PubMed          Journal:  Acta Biochim Pol        ISSN: 0001-527X            Impact factor:   2.149


  3 in total

1.  Enhancing the methanol tolerance of Candida antarctica lipase B by saturation mutagenesis for biodiesel preparation.

Authors:  Zhongbiao Tan; Xiangqian Li; Hao Shi; Xiulian Yin; Xiaoyan Zhu; Muhammad Bilal; Mary Mongina Onchari
Journal:  3 Biotech       Date:  2021-12-22       Impact factor: 2.406

Review 2.  Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET.

Authors:  Rita P Magalhães; Jorge M Cunha; Sérgio F Sousa
Journal:  Int J Mol Sci       Date:  2021-10-19       Impact factor: 5.923

Review 3.  The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties.

Authors:  Faez Iqbal Khan; Dongming Lan; Rabia Durrani; Weiqian Huan; Zexin Zhao; Yonghua Wang
Journal:  Front Bioeng Biotechnol       Date:  2017-03-09
  3 in total

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