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Literature summary 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

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

Inhibitors

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

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.9.3 Escherichia coli
-
-
-

Substrates and Products (Substrate)

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