Potent inhibition of the C-P lyase nucleosidase PhnI by Immucillin-A triphosphate

Siddhesh S. Kamat, Emmanuel S. Burgos, Frank M. Raushel

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)7366-7368
Number of pages3
Issue number42
StatePublished - Oct 22 2013

ASJC Scopus subject areas

  • Biochemistry


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