Oxalyl-CoA decarboxylase: breaking and making C-C bonds

Graduate Students Mini-Symposium

  • Date: Jan 7, 2019
  • Time: 02:25 PM (Local Time Germany)
  • Speaker: Simon Burgener
  • MPI Marburg, AG Erb
  • Location: MPI for Terrestrial Microbiology
  • Room: Lecture hall
  • Host: IMPRS
  • Contact: imprs@mpi-marburg.mpg.de

Oxalyl-Coenzyme A decarboxylase (OXC) from Methylobacterium extorquens catalyzes the thiamine pyrophosphate (ThDP) dependent decarboxylation of oxalyl-CoA, producing formyl-CoA and CO2. The reaction proceeds via a covalent intermediate on the ThDP cofactor. I demonstrated that the intermediate can be “trapped” with a broad range of aldehydes, creating a new C-C bond. Thus, OXC can not only catalyze C-C bond cleavage but also carboligation reactions. Interestingly, OXC can catalyze the carboligation starting from oxalyl-CoA as well as from formyl-CoA. The resulting products are 2-hydroxyacyl-CoA esters, which are very rare in natural metabolism, making them interesting intermediates for orthogonal synthetic metabolism.

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