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Literature summary for 2.7.1.11 extracted from

  • Fenton, A.W.; Paricharttanakul, N.M.; Reinhart, G.D.
    Identification of Substrate Contact Residues Important for the Allosteric Regulation of Phosphofructokinase from Escherichia coli (2003), Biochemistry, 42, 6453-6459.
    View publication on PubMed
Search for more literature for 2.7.1.11

Protein Variants

Protein Variants Comment Organism
E222A/H223A ability to be allosterically regulated is retained Escherichia coli
H249E ability to be allosterically regulated is retained, inhibition by phosphoenol pyruvate is lost Escherichia coli
M169A ability to be allosterically regulated is retained Escherichia coli
R162E ability to be allosterically regulated is retained Escherichia coli
R171E approx. 6% of wild-type catalytic activity Escherichia coli
R243E ability to be allosterically regulated is retained Escherichia coli
R252E allosteric response to MgATP2- is lost, inhibition by phosphoenol pyruvate is lost Escherichia coli
R72E approx. 0.5% of wild-type catalytic activity Escherichia coli
T125A almost no activity detectable Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.015
-
 fructose 6-phosphate pH 8.0, 8.5°C, T125A mutant PFK Escherichia coli
0.303
-
 fructose 6-phosphate pH 8.0, 8.5°C, R72E mutant PFK Escherichia coli
3.47
-
 fructose 6-phosphate pH 8.0, 8.5°C, R171E mutant PFK Escherichia coli
61
-
 fructose 6-phosphate pH 8.0, 8.5°C, wild-type PFK Escherichia coli