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 journalArticle

7 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)7366-7368
Number of pages3
JournalBiochemistry
Volume52
Issue number42
DOIs
StatePublished - 2013

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N-Glycosyl Hydrolases
Organophosphonates
Phosphates
Ribose
Adenine
Starvation
Bacteria
Adenosine Triphosphate
Substrates
carbon-phosphorus lyase
triphosphoric acid
immucillin A

ASJC Scopus subject areas

  • Biochemistry

Cite this

Potent inhibition of the C-P lyase nucleosidase PhnI by Immucillin-A triphosphate. / Kamat, Siddhesh S.; Burgos, Emmanuel S.; Raushel, Frank M.

In: Biochemistry, Vol. 52, No. 42, 2013, p. 7366-7368.

Research output: Contribution to journalArticle

Kamat, Siddhesh S. ; Burgos, Emmanuel S. ; Raushel, Frank M. / Potent inhibition of the C-P lyase nucleosidase PhnI by Immucillin-A triphosphate. In: Biochemistry. 2013 ; Vol. 52, No. 42. pp. 7366-7368.
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