Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.5 extracted from

  • Krug, U.; Patzschke, R.; Zebisch, M.; Balbach, J.; Straeter, N.
    Contribution of the two domains of E. coli 5'-nucleotidase to substrate specificity and catalysis (2013), FEBS Lett., 587, 460-466.
    View publication on PubMed
Search for more literature for 3.1.3.5

Protein Variants

Protein Variants Comment Organism
additional information individual expression of the N-terminal domain, amino acid residues Y26-V362, and the C-terminal domain, amino acid residues K363-Q550. The domains fold independently and properly. The C-terminal domain, which contains the substrate-binding pocket, is completely inactive while the N-terminal domain with the two-metal-ion-centers and the core catalytic residues exhibits significant activity, especially towards substrates with activated phosphate bonds such as ATP, ADP, 4-nitrophenyl phosphate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0129
-
 5'-AMP wild-type, pH 7.0, 22°C Escherichia coli
0.0209
-
 ATP wild-type, pH 7.0, 22°C Escherichia coli
0.0547
-
 ADP wild-type, pH 7.0, 22°C Escherichia coli
5.713
-
 4-nitrophenyl phosphate wild-type, pH 7.0, 22°C Escherichia coli
6.807
-
 ATP N-terminal protein domain, pH 7.0, 22°C Escherichia coli
10.15
-
 ADP N-terminal protein domain, pH 7.0, 22°C Escherichia coli
21.78
-
 4-nitrophenyl phosphate N-terminal protein domain, pH 7.0, 22°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Escherichia coli
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
 Escherichia coli 4-nitrophenol + phosphate
-
 ?
5'-AMP + H2O
-
 Escherichia coli adenosine + phosphate
-
 ?
ADP + 2 H2O
-
 Escherichia coli adenosine + 2 phosphate
-
 ?
ATP + 3 H2O
-
 Escherichia coli adenosine + 3 phosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
36.5
-
 ATP N-terminal protein domain, pH 7.0, 22°C Escherichia coli
40.8
-
 4-nitrophenyl phosphate wild-type, pH 7.0, 22°C Escherichia coli
45.6
-
 ADP N-terminal protein domain, pH 7.0, 22°C Escherichia coli
129
-
 4-nitrophenyl phosphate N-terminal protein domain, pH 7.0, 22°C Escherichia coli
459.1
-
 5'-AMP wild-type, pH 7.0, 22°C Escherichia coli
613.2
-
 ADP wild-type, pH 7.0, 22°C Escherichia coli
757
-
 ATP wild-type, pH 7.0, 22°C Escherichia coli

General Information

General Information Comment Organism
physiological function the two domains can be expressed individually in Escherichia coli and fold independently. The C-terminal domain, which contains the substrate-binding pocket, is completely inactive while the N-terminal domain with the two-metal-ion-centers and the core catalytic residues exhibits significant activity, especially towards substrates with activated phosphate bonds such as ATP, ADP, 4-nitrophenyl phosphate. The two domains do not reconstitute the full-length protein from the two folded individual domains Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.5
-
 ADP N-terminal protein domain, pH 7.0, 22°C Escherichia coli
5.4
-
 ATP N-terminal protein domain, pH 7.0, 22°C Escherichia coli
6.1
-
 4-nitrophenyl phosphate N-terminal protein domain, pH 7.0, 22°C Escherichia coli
7.1
-
 4-nitrophenyl phosphate wild-type, pH 7.0, 22°C Escherichia coli
11220
-
 ADP wild-type, pH 7.0, 22°C Escherichia coli
35600
-
 5'-AMP wild-type, pH 7.0, 22°C Escherichia coli
36200
-
 ATP wild-type, pH 7.0, 22°C Escherichia coli