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Literature summary extracted from

  • Heck, T.; Pham, P.H.; Hammes, F.; Thoeny-Meyer, L.; Richter, M.
    Continuous monitoring of enzymatic reactions on surfaces by real-time flow cytometry: sortase a catalyzed protein immobilization as a case study (2014), Bioconjug. Chem., 25, 1492-1500.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.22.70 additional information the SrtA variants SrtADELTAN59 and SrtADELTAN25, in which the N-terminal amino acid residues 1-59 and 1-25 of the native enzyme are truncated, perform very differently with regard to the immobilization reaction with green-fluorescent protein (GFPuv) on triglycine-modified polystyrene microbeads by the enzyme. While SrtADELTAN59 efficiently catalyzes the covalent attachment of GFPuv to the surface SrtADELTAN25 is essentially inactive. Besides the length of the N-terminal amino acid extension on the SrtA construct, the position of the His6-tag at either the N- or C-terminus affects the efficiency of enzymatic protein immobilization, overview. Three other mutants of SrtA show rapid initial attachment of the GFPuv target protein to the microbeads, with proceeding reaction time, cleavage of the covalently immobilized target protein from the surface prevails over the coupling reaction Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.70 Staphylococcus aureus
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Synonyms

EC Number Synonyms Comment Organism
3.4.22.70 SrtA
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Staphylococcus aureus