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A closer look at molecular mechanisms underlying inhibition of S -adenosyl-L-homocysteine hydrolase by transition metal cations.

Magdalena GawelPiotr H MaleckiJoanna SliwiakMarlena StepniewskaBarbara ImiolczykJustyna Czyrko-HorczakDorota JakubczykŁukasz MarczakMarta Eliza Plonska-BrzezinskaKrzysztof Brzezinski
Published in: Chemical communications (Cambridge, England) (2024)
We report biochemical and structural studies on inhibiting bacterial S -adenosyl-L-homocysteine hydrolase by transition metal cations. Our results revealed diverse molecular mechanisms of enzyme inactivation. Depending on the cation, the mechanism is based on arresting the enzyme in its closed, inactive conformation, disulfide bond formation within the active site or oxidation of the intermediate form of a cofactor.
Keyphrases
  • transition metal
  • ionic liquid
  • signaling pathway
  • hydrogen peroxide
  • single cell
  • molecular dynamics simulations
  • crystal structure
  • nitric oxide