Potent Inhibition of the C-P Lyase Nucleosidase Phnl by Immucillin-A Triphosphate | Academic Article individual record
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.

author list (cited authors)
Kamat, S. S., Burgos, E. S., & Raushel, F. M.
publication date
2013
published in
BIOCHEMISTRY Journal
keywords
  • Catalysis
  • Models, Chemical
  • Pyrrolidines
  • Organophosphonates
  • Lyases
  • Escherichia Coli
  • Pentosephosphates
  • Adenosine Triphosphate
  • Adenine
  • Magnesium
  • Polyphosphates
  • Escherichia Coli Proteins
altmetric score

8.08

citation count

9