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The 2-methylcitric acid cycle (2-MCC) is a common route of propionate catabolism in microorganisms. In  Salmonella enterica , the  prpBCDE  operon encodes most of the 2-MCC enzymes. In other organisms,  e . g .,  Shewanella oneidensis  MR-1, two genes,  acnD  and  prpF  replace  prpD , which encodes 2-methylcitrate dehydratase. We showed that together,  S .  oneidensis  AcnD and PrpF ( So AcnD,  So PrpF) compensated for the absence of PrpD in a  S .  enterica prpD  strain. We also showed that  So AcnD had 2-methylcitrate dehydratase activity and that PrpF has aconitate isomerase activity. Here we report  in vitro  evidence that the product of the  So AcnD reaction is an isomer of 2-methyl- cis -aconitate (2-MCA], the product of the  Se PrpD reaction. We show that the  So PrpF protein isomerizes the product of the AcnD reaction into the PrpD product (2-MCA], a known substrate of the housekeeping aconitase (AcnB]. Given that  So PrpF is an isomerase, that  So AcnD is a dehydratase, and the results from  in vivo  and  in vitro  experiments reported here, it is likely that 4-methylaconitate is the product of the AcnD enzyme. Results from  in vivo  studies using a  S .  enterica prpD  strain show that  So PrpF variants with substitutions of residues K73 or C107 failed to support growth with propionate as the sole source of carbon and energy. High-resolution (1.22 Å) three-dimensional crystal structures of PrpF K73E  in complex with  trans- aconitate or malonate provide insights into the mechanism of catalysis of the wild-type protein.

plos one

The PrpF protein of Shewanella oneidensis MR-1 catalyzes the isomerization of 2-methyl-cis-aconitate during the catabolism of propionate via the AcnD-dependent 2-methylcitric acid cycle