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Literature summary for 2.4.2.3 extracted from

  • Oliva, I.; Zuffi, G.; Barile, D.; Orsini, G.; Tonon, G.; De Gioia, L.; Ghisotti, D.
    Characterization of Escherichia coli uridine phosphorylase by single-site mutagenesis (2004), J. Biochem., 135, 495-499.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E196A complete loss of uridine phosphorylase activity Escherichia coli
E198D complete loss of uridine phosphorylase activity Escherichia coli
E198G complete loss of uridine phosphorylase activity Escherichia coli
E198Q complete loss of uridine phosphorylase activity Escherichia coli
F162A mutation causes a drastic decrease in uridine phosphorylase activity Escherichia coli
H8A mutation lowers the activity by 20% Escherichia coli
I69A mutation does not decrease activity Escherichia coli
M197A low activity conserved Escherichia coli
M197S low activity conserved Escherichia coli
R30A complete loss of uridine phosphorylase activity Escherichia coli
R30K very low activity Escherichia coli
R91A complete loss of uridine phosphorylase activity Escherichia coli
R91K very low activity Escherichia coli
T94A mutation causes a drastic decrease in uridine phosphorylase activity Escherichia coli
W196D mutant enzyme is still partially active Escherichia coli
Y195A increase in activity Escherichia coli
Y195G mutation causes a drastic decrease in uridine phosphorylase activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P12758
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