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Literature summary for 3.1.3.48 extracted from

  • Zhang, Z.Y.
    Chemical and mechanistic approaches to the study of protein tyrosine phosphatases (2003), Acc. Chem. Res., 36, 385-392.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D356N dramatically reduced activity, D356 acts as general acid/base Yersinia enterocolitica
additional information overview Yersinia enterocolitica
R409A dramatical decrease in kcat, 26-fold increase in Km-value Yersinia enterocolitica
R409K dramatical decrease in kcat, 1.9-fold increase in Km-value Yersinia enterocolitica

Inhibitors

Inhibitors Comment Organism Structure
additional information overview, development of inhibitors Yersinia enterocolitica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Yersinia enterocolitica essential for virulence of the bacteria responsible for the plague ?
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?

Organism

Organism UniProt Comment Textmining
Yersinia enterocolitica
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Reaction

Reaction Comment Organism Reaction ID
[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate mechanism, transition state of reaction, kinetic isotope effects, overview Yersinia enterocolitica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information essential for virulence of the bacteria responsible for the plague Yersinia enterocolitica ?
-
?