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Literature summary for 2.7.1.11 extracted from

  • Wang, X.; Kemp, R.G.
    Reaction path of phosphofructo-1-kinase is altered by mutagenesis and alternative substrates (2001), Biochemistry, 40, 3938-3942.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
M169A 142fold lower kcat than wild-type Escherichia coli
M169L 6fold lower kcat than wild-type Escherichia coli
R25S not activated by GDP, pattern of ATP inhibition nearly identical to wild-type Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ATP inhibition of fructose 1-phosphate phosphorylation above 0.08 mM ATP Escherichia coli
additional information no substrate inhibition with gamma-thio-ATP Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
ATP pH 7.2, 30°C, cosubstrate fructose 1-phosphate Escherichia coli
0.096
-
D-fructose 6-phosphate pH 7.2, 30°C, cosubstrate gamma-thio-ATP Escherichia coli
0.1
-
ATP pH 7.2, 30°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A796
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-carboxymethyl-ATP + D-fructose 6-phosphate 90% of activity with with ATP Escherichia coli 1-carboxymethyl-ADP + D-fructose 1,6-bisphosphate
-
?
ATP + fructose 1-phosphate 60fold lower kcat than with fructose 6-phosphate Escherichia coli ADP + fructose 1,6-bisphosphate
-
?
gamma-thio-ATP + fructose 6-phosphate 3000fold lower kcat than with ATP Escherichia coli ADP + fructose 1-thio-phosphate-6-phosphate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.016
-
D-fructose 6-phosphate pH 7.2, 30°C, cosubstrate gamma-thio-ATP Escherichia coli
49
-
fructose 6-phosphate pH 7.2, 30°C, cosubstrate ATP Escherichia coli
88
-
fructose 6-phosphate pH 7.2, 30°C, at 2mM ATP Escherichia coli