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Inside back cover

Catalysis Science & Technology Vol - 4 Issue - 8

Catalysis Science & Technology Vol - 4 Issue - 7

Catalysis Science & Technology Vol - 4 Issue - 6

Catalysis Science & Technology Vol - 4 Issue - 5

Catalysis Science & Technology Vol - 4 Issue - 4

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Catalysis Science & Technology Vol -1

Sortase A catalyzed reaction pathways: a comparative study with six SrtA variants

Content Provider	Royal Society of Chemistry (RSC)
Author	Richter, Michael Yerlikaya, Alpaslan Heck, Tobias Pham, Phu-Huy Thöny-Meyer, Linda
Copyright Year	2014
Abstract	Sortase A from Staphylococcus aureus (SrtA) has emerged as a useful enzymatic tool to covalently link proteins in a site-directed manner. Despite the proposed specificity of the SrtA-catalyzed reaction for target proteins carrying the amino acid motif LPXTG, enzymatic side reactions are frequently encountered impairing the yield and purity of the transpeptidation product. In this comparative study we investigated reactions of six different variants of SrtA with soluble protein substrates. Besides the transpeptidation reaction generating the desired heterodimeric product, all tested SrtA variants also catalyzed the formation of byproducts (i.e. homooligomeric and hydrolyzed species of the target protein) to different extents. We found that not only the choice of the enzyme, but also the composition and the context of the sorting motif within the particular amino acid sequence of the target protein had a critical impact on the apparent initial rates of the coupling reactions. In addition to the natural sorting signal LPETG, the motif LAETG was also recognized by the investigated SrtA variants. Even though the overall coupling rates with the LAETG-containing target proteins were rather slow, the formation of unwanted byproducts was largely suppressed under these conditions.
Starting Page	2946
Ending Page	2956
Page Count	11
File Format	HTM / HTML PDF
ISSN	20444753
Volume Number	4
Issue Number	9
Journal	Catalysis Science & Technology
DOI	10.1039/c4cy00347k
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Sortase A Aureus Carboxylic acid Enzyme Protein targeting Site-directed mutagenesis Protein
Content Type	Text
Resource Type	Article
Subject	Catalysis

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Site-directed mutagenesis of glutamate 317 of bovine alpha-1,3Galactosyltransferase and its effect on enzyme activity: implications for reaction mechanism.

Mutagenesis Studies of Substrate Recognition and Catalysis in the Sortase A Transpeptidase from Staphylococcus aureus

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Structure of the Bacillus anthracis Sortase A Enzyme Bound to Its Sorting Signal A FLEXIBLE AMINO-TERMINAL APPENDAGE MODULATES SUBSTRATE ACCESS

Sortase A catalyzed reaction pathways: a comparative study with six SrtA variants

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