Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

Crystallization and preliminary X-ray analysis of UMP/CMP-kinase from Dictyostelium discoideum with the specific bisubstrate inhibitor P1-(adenosine 5′)-P5-(uridine 5′)-pentaphosphate (UP5A)

MPG-Autoren
/persons/resource/persons123197

Wiesmüller,  Lisa
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95148

Scheffzek,  Klaus
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons93802

Kliche,  Werner
Emeritus Group Bioorganic Chemistry, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons93142

Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95966

Wittinghofer,  Alfred
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons94928

Reinstein,  Jochen
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Wiesmüller, L., Scheffzek, K., Kliche, W., Goody, R. S., Wittinghofer, A., & Reinstein, J. (1995). Crystallization and preliminary X-ray analysis of UMP/CMP-kinase from Dictyostelium discoideum with the specific bisubstrate inhibitor P1-(adenosine 5′)-P5-(uridine 5′)-pentaphosphate (UP5A). FEBS Letters, 363(1), 22-24. doi:10.1016/0014-5793(95)00271-A.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002C-4231-8
Zusammenfassung
UMP/ICMP-kinase (UK) from the slime mold Dictyostelium discoideum has been purified to high homogeneity and co-crystallized with the bisubstrate inhibitor P1-(adenosine 5′)-P5-(uridine 5′)-pentaphosphate (UP5A). UP5A binds to UK with a dissociation constant (K d ) of 3 ± 0.5 nM at 25°C and pH 7.5. This is some 50-fold tighter than the binding of P1,P5-(diadenosine 5′)-pentaphosphate (AP5A, K d = 160 ± 15 nM). AP5A is a bisubstrate inhibitor that is specific for adenylate kinase. The crystals have the symmetry of the tetragonal space group P41212 or its enantiomorph P43212. The unit cell dimensions are math formula. The crystals diffract to a Bragg spacing of 2.1 Å.