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Literature summary extracted from

  • Völlmecke, C.; Kötting, C.; Gerwert, K.; Lübben, M.
    Spectroscopic investigation of the reaction mechanism of CopB-B, the catalytic fragment from an archaeal thermophilic ATP-driven heavy metal transporter (2009), FEBS J., 276, 6172-6186.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.2.9 Mg2+ not necessary for nucleotide association but essential for the phosphatase activity Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.9 Saccharolobus solfataricus Q97UU7
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.9 additional information study of the mechanism of ATP hydrolysis of a shortened variant of the heavy metal-translocating P-type ATPase CopB. Stoichiometric high-affinity binding of one nucleotide to the protein is demonstrated. The phosphate groups are not involved in nucleotide binding. A model of the hydrolytic mechanism is suggested Saccharolobus solfataricus ?
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Synonyms

EC Number Synonyms Comment Organism
7.2.2.9 CopV
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Saccharolobus solfataricus