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The novel fluorescent CDP-analogue (Pβ)MABA-CDP is a specific probe for the NMP binding site of UMP/CMP kinase

  • MARKUS G. RUDOLPH (a1), THOMAS J.H. VEIT (a1) and JOCHEN REINSTEIN (a1)

Abstract

Direct thermodynamic and kinetic investigations of the binding of nucleotides to the nucleoside monophosphate (NMP) site of NMP kinases have not been possible so far because a spectroscopic probe was not available. By coupling a fluorescent N-methylanthraniloyl- (mant) group to the β-phosphate of CDP via a butyl linker, a CDP analogue [(Pβ)MABA-CDP] was obtained that still binds specifically to the NMP site of UmpKdicty, because the base and the ribose moieties, which are involved in specific interactions, are not modified. This allows the direct determination of binding constants for its substrates in competition experiments.

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Corresponding author

Reprint requests to: Jochen Reinstein, Max-Planck-Institut für Molekulare Physiologie, Abetilung Physikalische Biochemie, Otto-Hahn-Strasse 11, 44227 Dormund, Germany; e-mail: joachim.reinstein@mpi-dortmund.mpg.de.

Keywords

The novel fluorescent CDP-analogue (Pβ)MABA-CDP is a specific probe for the NMP binding site of UMP/CMP kinase

  • MARKUS G. RUDOLPH (a1), THOMAS J.H. VEIT (a1) and JOCHEN REINSTEIN (a1)

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