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Literature summary for 7.2.2.21 extracted from

  • Bal, N.; Wu, C.C.; Catty, P.; Guillain, F.; Mintz, E.
    Cd2+ and the N-terminal metal-binding domain protect the putative membranous CPC motif of the Cd2+-ATPase of Listeria monocytogenes (2003), Biochem. J., 369, 681-685.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.21

Cloned(Commentary)

Cloned (Comment) Organism
expression in Sf9 cells of the native enzyme and a truncated peptide lacking the metal-binding domain Listeria monocytogenes

Inhibitors

Inhibitors Comment Organism Structure
N-ethylmaleimide inhibits the formation of the phosphoenzyme, effect can be supressed in presence of Cd2+ Listeria monocytogenes

Organism

Organism UniProt Comment Textmining
Listeria monocytogenes
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + Cd2+[side 1] = ADP + phosphate + Cd2+[side 2] ATP forms first a phosphoenzyme which transports the metal across the membrane Listeria monocytogenes
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Cd2+/in
-
 Listeria monocytogenes ADP + phosphate + Cd2+/out
-
 ?

Synonyms

Synonyms Comment Organism
CadA
-
 Listeria monocytogenes