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Literature summary extracted from

  • Piotukh, K.; Geltinger, B.; Heinrich, N.; Gerth, F.; Beyermann, M.; Freund, C.; Schwarzer, D.
    Directed evolution of sortase A mutants with altered substrate selectivity profiles (2011), J. Am. Chem. Soc., 133, 17536-17539.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.22.70 C184A catalytically inactive Staphylococcus aureus
3.4.22.70 additional information the F40-sortase mutant loses activity compared to the wild type enzyme and prefers ligation of the FPxTG motif over the native LPxTG sequence. The F40-sortase possesses a remarkable broad selectivity and accepted aromatic amino acids as well as residues with small side chains, including Ala, Asp, Ser, Pro, and Gly, at position 1 of the sorting motif Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.70 Staphylococcus aureus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.70 5(6)-carboxyfluorescein-6-aminohexanoic acid-LPKTGGRR-NH2 + H2O
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Staphylococcus aureus ?
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