Localization of catalytic active sites in the large cytoplasmic domain of Na+/K+-ATPase

Annals of the New York Academy of Sciences

Volumn 986, Issue , 2003, Pages 242-244

  Krumscheid, Rita ^a   Suánková, Klára ^b   Ettrich, Rüdiger ^c   Teisinger, Jan ^b   Amler, Even ^b   Schoner, Wilhelm ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

^b INSTITUTE OF PHYSIOLOGY   (Czech Republic)

^c UNIVERSITY OF SOUTH BOHEMIA   (Czech Republic)

Author keywords

H4H5 loop; Phosphatase activity; TNP ATP

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATASE (POTASSIUM);

CATALYSIS; CATALYST; CONFERENCE PAPER; CYTOPLASM; ENZYME ACTIVITY; HYDROLYSIS; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION;

EID: 0037565176     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2003.tb07171.x     Document Type: Conference Paper

References (4)

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3. +-ATPase deduced by restraint-based comparative modeling shows only one ATP-binding site. J. Mol. Model. 7: 184-192.
4. TRAN, C.M. & R.A. FARLEY. 1999. Catalytic activity of an isolated domain of Na,K-ATPase expressed in Escherichia coli. Biophys. J. 77: 258-266.