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Literature summary for 3.1.3.5 extracted from

  • McMillen, L.; Beacham, I.R.; Burns, D.M.
    Cobalt activation of Escherichia coli 5'-nucleotidase is due to zinc ion displacement at only one of two metal-ion-binding sites (2003), Biochem. J., 372, 625-630.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
D41N specific activity of the mutant enzyme is 9.1% of the wild-type enzyme, activation by Co2+ is less than 2fold the level of activation of the wild-type enzyme Escherichia coli
D84N mutant enzyme exhibits 900fold decreased specific activity and increased level of activation by Co2+, 2700fold compared with approximately 40fold for the wild-type enzyme Escherichia coli
E118Q specific activity of the mutant enzyme is 6.1% of the wild-type enzyme, activation by Co2+ is 2.5fold the level of activation of the wild-type enzyme Escherichia coli
H117N specific activity of the mutant enzyme is 0.037% of the wild-type activity in presence of Co2+ and 0.042% of the wild-type activity in absence of Co2+ Escherichia coli
H217N specific activity of the mutant enzyme is 0.23% of the wild-type enzyme. Activation by Co2+ is approximately 6fold the level of activation of the wild-type enzyme Escherichia coli
H43N specific activity of the mutant enzyme is 0.76% of the wild-type enzyme, activation by Co2+ is 4fold less than the activation of the wild-type enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activation is due to zinc ion displacement at only one of two metal-ion-binding sites, displacement occurs at the metal-ion bionding site consisting of the residues Asp84, Asn116, His217 and His252. Km for wild-type enzyme: 0.0925 mM Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli