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Literature summary for 3.1.3.5 extracted from

  • Schultz-Heienbrok, R.; Maier, T.; Strater, N.
    A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5'-nucleotidase (2005), Biochemistry, 44, 2244-2252.
    View publication on PubMed
Search for more literature for 3.1.3.5

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol mutant P90C/L424C, 2fold activation, mutant S228C/P513C, 250fold activation Escherichia coli

Protein Variants

Protein Variants Comment Organism
P90C/L424C enzyme variant that can adopt a closed and a half open conformation, active in oxidized state Escherichia coli
S228C/P513C enzyme variant trapped in open conformation, almost inactive, but up to 250fold activation by reduction of disulfide bridge Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
5'-AMP
-
 Escherichia coli
additional information no substrate inhibition by p-nitrophenyl phosphate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
 5'-AMP mutant P90C/L424C, pH 7.5, 25°C Escherichia coli
0.074
-
 5'-AMP wild-type, pH 7.5, 25°C Escherichia coli
4.741
-
 p-nitrophenyl phosphate wild-type-type, pH 7.5, 25°C Escherichia coli
5.355
-
 p-nitrophenyl phosphate mutant P90C/L424C, pH 7.5, 25°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
CoCl2 added to all kinetic measurements Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P07024
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-AMP + H2O
-
 Escherichia coli adenosine + phosphate
-
 ?
p-nitrophenyl phosphate + H2O
-
 Escherichia coli p-nitrophenol + phosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
60
-
 p-nitrophenyl phosphate wild-type-type, pH 7.5, 25°C Escherichia coli
313
-
 5'-AMP mutant P90C/L424C, pH 7.5, 25°C Escherichia coli
350
-
 p-nitrophenyl phosphate mutant P90C/L424C, pH 7.5, 25°C Escherichia coli
750
-
 5'-AMP wild-type, pH 7.5, 25°C Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6
-
 5'-AMP mutant P90C/L424C, pH 7.5, 25°C Escherichia coli
23
-
 5'-AMP wild-type, pH 7.5, 25°C Escherichia coli