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Article

Directed evolution of sortase A mutants with altered substrate selectivity profiles.

Journal of the American Chemical Society - 9 Nov 2011

Piotukh Kirill, Geltinger Bernhard, Heinrich Nadja, Gerth Fabian, Beyermann Michael, Freund Christian, Schwarzer Dirk

Abstract excerpt

The ligation of two polypeptides in a chemoselective manner by the bacterial transpeptidase sortase A has become a versatile tool for protein engineering approaches. When sortase-mediated ligation is used for protein semisynthesis, up to four mutations resulting from the strict requirement of the LPxTG sorting motif are introduced into the target protein. Here we report the directed evolution of a mutant sortase...

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Identifiers

PMID: 21978125
DOI: 10.1021/ja205630g

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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