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SpyTag/SpyCatcher Cyclization Enhances the Thermostability of Firefly Luciferase

SpyTag/SpyCatcher Cyclization Enhances the Thermostability of Firefly Luciferase

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1822391815

SpyTag/SpyCatcher Cyclization Enhances the Thermostability of Firefly Luciferase

About this item

Full title

SpyTag/SpyCatcher Cyclization Enhances the Thermostability of Firefly Luciferase

Publisher

United States: Public Library of Science

Journal title

PloS one, 2016-09, Vol.11 (9), p.e0162318-e0162318

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

SpyTag can spontaneously form a covalent isopeptide bond with its protein partner SpyCatcher. Firefly luciferase from Photinus pyralis was cyclized in vivo by fusing SpyCatcher at the N terminus and SpyTag at the C terminus. Circular LUC was more thermostable and alkali-tolerant than the wild type, without compromising the specific activity. Struct...

Alternative Titles

Full title

SpyTag/SpyCatcher Cyclization Enhances the Thermostability of Firefly Luciferase

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1822391815

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1822391815

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0162318

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