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Literature summary extracted from

  • Garcia, L.; Chayet, L.; Kettlun, A.M.; Collados, L.; Chiong, M.; Traverso-Cori, A.; Mancilla, M.; Valenzuela, M.A.
    Kinetic characteristics of nucleoside mono-, di- and triphosphate activities of the periplasmic 5'-nucleotidase of Escherichia coli (1997), Comp. Biochem. Physiol. B, 117, 135-142.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.5 ATP
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.5 0.66
-
 5'-IMP
-
 Escherichia coli
3.1.3.5 1
-
 5'-GMP
-
 Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.5 periplasm
-
 Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.5 5'-AMP + H2O Escherichia coli enzyme in the system for the hydrolysis of extracellular nucleotides so that product nucleosides are readily transported into the cell ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.5 Escherichia coli
-
 multifunctional enzyme with an apyrase-like activity, EC 3.6.1.5
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.5
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.5 5'-AMP + H2O
-
 Escherichia coli adenosine + phosphate
-
 ?
3.1.3.5 5'-AMP + H2O enzyme in the system for the hydrolysis of extracellular nucleotides so that product nucleosides are readily transported into the cell Escherichia coli ?
-
 ?
3.1.3.5 5'-GMP + H2O
-
 Escherichia coli guanosine + phosphate
-
 ?
3.1.3.5 5'-IMP + H2O
-
 Escherichia coli inosine + phosphate
-
 ?