Potent inhibition of the C-P lyase nucleosidase PhnI by Immucillin-A triphosphate. Academic Article uri icon

abstract

  • The C-P lyase complex in bacteria catalyzes the transformation of phosphonates to orthophosphate under conditions of phosphate starvation. The first committed step in the C-P lyase-catalyzed reaction is the displacement of adenine from MgATP by phosphonate substrates, yielding ribose-1-phosphonate-5-triphosphate. In the C-P lyase complex, this reaction is catalyzed by the nucleosidase PhnI and modulated by the addition of PhnG, PhnH, and PhnL. Here we describe the synthesis of Immucillin-A triphosphate, a mimic of the transition state structure for the nucleosidase reaction catalyzed by PhnI. This compound inhibits PhnI with a dissociation constant of 20 nM at pH 7.5.

published proceedings

  • Biochemistry

altmetric score

  • 8.08

author list (cited authors)

  • Kamat, S. S., Burgos, E. S., & Raushel, F. M.

citation count

  • 10

complete list of authors

  • Kamat, Siddhesh S||Burgos, Emmanuel S||Raushel, Frank M

publication date

  • October 2013