Intermediate Phosphorylation Reactions in the Mechanism of ATP Utilization by the Copper ATPase (CopA) of Thermotoga maritima

Recombinant and purified Thermotoga maritima CopA sustains ATPase velocity of 1.78–2.73 μmol/mg/min in the presence of Cu(+) (pH 6, 60 °C) and 0.03–0.08 μmol/mg/min in the absence of Cu(+). High levels of enzyme phosphorylation are obtained by utilization of [γ-(32)P]ATP in the absence of Cu(+). Thi...

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Detalles Bibliográficos
Autores principales: Hatori, Yuta, Hirata, Ayami, Toyoshima, Chikashi, Lewis, David, Pilankatta, Rajendra, Inesi, Giuseppe
Formato: Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2008
Materias:
Membrane Transport, Structure, Function, and Biogenesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2504886/
https://www.ncbi.nlm.nih.gov/pubmed/18562314
http://dx.doi.org/10.1074/jbc.M802735200

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2504886/
https://www.ncbi.nlm.nih.gov/pubmed/18562314
http://dx.doi.org/10.1074/jbc.M802735200

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