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Literature summary for 7.2.2.12 extracted from

  • Okkeri, J.; Laakkonen, L.; Haltia, T.
    The nucleotide-binding domain of the Zn2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP (2004), Biochem. J., 377, 95-105.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
A508F at low ATP concentrations the mutant enzyme is poorly phosphorylated Escherichia coli
G444V mutation stabilizes the E2-P state. Gly144 might become close to P upon domain movements Escherichia coli
G503S at low ATP concentrations the mutant enzyme is poorly phosphorylated. The phosphorylation defect of the mutant enzyme can be partially compensated by using higher ATP concentrations Escherichia coli
G505R at low ATP concentrations the mutant enzymeis poorly phosphorylated. The phosphorylation defect of the mutant enzyme can be fully compensated by using higher ATP concentrations Escherichia coli
H475A mutant enzyme reacts poorly with ATP, mutation influences the binding of ATP and also other catalytic steps Escherichia coli
H475D mutant enzyme reacts poorly with ATP, mutation influences the binding of ATP and also other catalytic steps Escherichia coli
H475L mutant enzyme reacts poorly with ATP, mutation influences the binding of ATP and also other catalytic steps Escherichia coli
H475S mutant enzyme reacts poorly with ATP, mutation influences the binding of ATP and also other catalytic steps Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Zn2+/in
-
 Escherichia coli ADP + phosphate + Zn2+/out
-
 ?

Synonyms

Synonyms Comment Organism
Zn2+-transporting P-type ATPase
-
 Escherichia coli