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Article

Semisynthesis and initial characterization of sortase A mutants containing selenocysteine and homocysteine.

Bioorganic & medicinal chemistry - 15 Jun 2015

Schmohl Lena, Wagner Felix Roman, Schümann Michael, Krause Eberhard, Schwarzer Dirk

Abstract excerpt

The bacterial transpeptidase sortase A is a well-established tool in protein chemistry and catalyzes the chemoselective ligation of peptides and proteins. During catalysis sortase A cleaves the conserved Leu-Pro-X-Thr-Gly sorting motif at the Thr residue under concomitant thioester formation at active site Cys184. We have used expressed protein ligation (EPL) to generate sortase mutants with Cys184 replaced by...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 25900629
DOI: 10.1016/j.bmc.2015.03.057

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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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