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Amino Acids, Peptides, and Proteins > Proteins > Carrier Proteins > Membrane Transport Proteins > P-type ATPases
Amino Acids, Peptides, and Proteins > Proteins > Membrane Proteins > Membrane Transport Proteins > P-type ATPases
... > Enzymes and Coenzymes > Enzymes > Hydrolases > Acid Anhydride Hydrolases > Adenosine Triphosphatases > P-type ATPases

Käytettävä termi

P-type ATPases  

Tyyppi

  • Topical Descriptor

Yläkäsite

Alakäsitteet

Ohjaustermit

  • Adenosine Triphosphatase, P-type
  • Adenosine Triphosphatases, Phosphorylation-type
  • Adenosine Triphosphatases, P-type
  • ATPase, E1-E2
  • Atpase, P Type
  • ATPase, P-type
  • ATPases, E1-E2
  • ATPases, Phosphorylation-type
  • E1 E2 ATPase
  • E1-E2 ATPase
  • E1 E2 ATPases
  • E1-E2 ATPases
  • Phosphorylation type Adenosine Triphosphatases
  • Phosphorylation-type Adenosine Triphosphatases
  • Phosphorylation type ATPases
  • Phosphorylation-type ATPases
  • P type Adenosine Triphosphatase
  • P-type Adenosine Triphosphatase
  • P type Adenosine Triphosphatases
  • P-type Adenosine Triphosphatases
  • P Type Atpase
  • P-type ATPase
  • Triphosphatase, P-type Adenosine
  • Triphosphatases, Phosphorylation-type Adenosine
  • Triphosphatases, P-type Adenosine
  • Type Atpase, P

Käyttöhuomautus

  • A highly conserved family of ATPases that facilitate the transport of lipids and cations across the plasma membrane. Structurally, they are elongated ALPHA-HELICES constituting five functionally distinct domains: three cytoplasmic domains A, N, and P which contain the catalytic sites, and two transmembrane domains. The N domain phosphorylates the P-domain at an invariant ASPARTATE residue, which, in turn, is dephosphorylated by the A domain. The phosphorylation and dephosphorylation cycles drive conformational changes in the protein between two states (E1 and E2), which allow the substrate to access the other side of the membrane.

Huomautus muutoshistoriasta

  • 2018

Muunkieliset termit

URI

http://www.yso.fi/onto/mesh/D000073779

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RDF/XML TURTLE JSON-LD Luotu 11.7.2017, viimeksi muokattu 30.6.2021