Characterization, crystallization and two three dimensional structures of the N10- formyltetrahydrofolate synthetase (FTHFS) from the syntrophic acetate oxidizing bacterium Tepidanaerobacter acetatoxydans Re1

Abstract: The crystal structure of N10- formyltetrahydrofolate synthetase 1 (FTHFS 1) and N10- formyltetrahydrofolate synthetase 2 (FTHFS 2) from the syntrophic acetate oxidizing bacterium, Tepidanaerobacter acetatoxydans Re1, was solved by x-ray crystallography to a resolution of 2.15 Å, and 2.30 Å resolution, respectively. The FTHFS 1 crystal structure has four non-crystallographic related protein molecules in the asymmetric unit of the crystal, while FTHFS 2 has two. The pH optimum in the formylation reaction for FTHFS 1 was determined to be 7.5, while FTHFS 2 had a pH optimum of 9, and it was determined that both enzymes had a temperature optimum of 60°C for their formulation reactions. An attempt to perform the deformylation reaction with both enzymes was unsuccessfully carried out.