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Literature summary for 2.7.9.3 extracted from

  • Kim, I.Y.; Stadtman, T.C.
    Effects of monovalent cations and divalent metal ions on Escherichia coli selenophosphate synthetase (1994), Proc. Natl. Acad. Sci. USA, 91:, 7326-7329.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
C17S in mutants C17S and C19S the binding of MnATP2- is unaffected by Zn2+ Escherichia coli
C19S in mutants C17S and C19S the binding of MnATP2- is unaffected by Zn2+ Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Li+ in presence of K+ Escherichia coli
Na+ in presence of K+ Escherichia coli
Zn2+ decreases binding of Mn-ATP2- to the enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
K+ essential for catalytic reaction Escherichia coli
Mg2+ required Escherichia coli
Mn2+ MnATP2-, although not able to replace MgATP2- for catalytic activity, binding to the enzyme in presence of K+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + selenide + H2O
-
Escherichia coli AMP + selenophosphate + phosphate
-
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