Revisiting AMPylation through the lens of Fic enzymes

Burak Gulen, Aymelt Itzen

Research output: Contribution to journalReview articlepeer-review

3 Scopus citations


AMPylation, a post-translational modification (PTM) first discovered in the late 1960s, is catalyzed by adenosine monophosphate (AMP)-transferring enzymes. The observation that filamentation-induced-by-cyclic-AMP (fic) enzymes are associated with this unique PTM revealed that AMPylation plays a major role in hijacking of host signaling by pathogenic bacteria during infection. Studies over the past decade showed that AMPylation is conserved across all kingdoms of life and, outside their role in infection, also modulates cellular functions. Many aspects of AMPylation are yet to be uncovered. In this review we present the advancement in research on AMPylation and Fic enzymes as well as other distinct classes of enzymes that catalyze AMPylation.

Original languageEnglish
Pages (from-to)350-363
Number of pages14
JournalTrends in Microbiology
Issue number4
StatePublished - Apr 2022
Externally publishedYes


  • AMPylation
  • Fic enzymes
  • host–pathogen interactions
  • post-translational modifications
  • pseudokinases


Dive into the research topics of 'Revisiting AMPylation through the lens of Fic enzymes'. Together they form a unique fingerprint.

Cite this