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Biochemical properties and crystal structure of formate-tetrahydrofolate ligase from Methylobacterium extorquens CM4
Ist Teil von
Biochemical and biophysical research communications, 2020-07, Vol.528 (3), p.426-431
Ort / Verlag
United States: Elsevier Inc
Erscheinungsjahr
2020
Link zum Volltext
Quelle
MEDLINE
Beschreibungen/Notizen
Methylobacterium extorquens is a methylotroph model organism that has the ability to assimilate formate using the tetrahydrofolate (THF) pathway. The formate-tetrahydrofolate ligase from M. extorquens (MeFtfL) is an enzyme involved in the THF pathway that catalyzes the conversion of formate, THF, and ATP into formyltetrahydrofolate and ADP. To investigate the biochemical properties of MeFtfL, we evaluated the metal usage and enzyme kinetics of the enzyme. MeFtfL uses the Mg ion for catalytic activity, but also has activity for Mn and Ca ions. The enzyme kinetics analysis revealed that Km value of farmate was much higher than THF and ATP, which shows that the ligation activity of MeFtfL is highly dependent on formation concentration. We also determined the crystal structure of MeFtfL at 2.8 Å resolution. MeFtfL functions as a tetramer, and each monomer consists of three domains. The structural superposition of MeFtfL with FtfL from Moorella thermoacetica allowed us to predict the substrate binding site of the enzyme.
•The kinetics properties and metal ion usage of FtfL from M. extorquens CM4 (MeFtfL) were investigated.•The crystal structure of MeFtfL was determined.•The substrate binding mode of MeFtfL was elucidated.