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Literature summary for 2.5.1.7 extracted from

  • Thomas, A.M.; Ginj, C.; Jelesarov, I.; Amrhein, N.; Macheroux, P.
    Role of K22 and R120 in the covalent binding of the antibiotic fosfomycin and the substrate-induced conformational change in UDP-N-acetylglucosamine enolpyruvyl transferase (2004), Eur. J. Biochem., 271, 2682-2690.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K22E 0.05% of wild-type activity, no formation of covalent adduct with fosfomycin Enterobacter cloacae
K22R 0.3% of wild-type activity Enterobacter cloacae
K22V 0.03% of wild-type activity, similar to wild-type in binding of fosfomycin, presence of UDP-N-acetylglucosamine required Enterobacter cloacae
K22V/R120K no residual activity, heat capacity changes are markedly redcued Enterobacter cloacae
K22V/R120V no residual activity Enterobacter cloacae
R120K less than 0.05% of wild-type activity, heat capacity changes are markedly redcued Enterobacter cloacae

Inhibitors

Inhibitors Comment Organism Structure
fosfomycin irreversible, alkylation of C115 Enterobacter cloacae

Organism

Organism UniProt Comment Textmining
Enterobacter cloacae P33038
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