Literature summary extracted from
Ogwang, S.; Nguyen, H.T.; Sherman, M.; Bajaksouzian, S.; Jacobs, M.R.; Boom, W.H.; Zhang, G.F.; Nguyen, L.
Bacterial conversion of folinic acid is required for antifolate resistance (2011), J. Biol. Chem., 286, 15377-15390.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
6.3.3.2 |
expression in Escherichia coli |
Mycolicibacterium smegmatis |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
6.3.3.2 |
Mycolicibacterium smegmatis |
A0R3H2 |
- |
- |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
6.3.3.2 |
physiological function |
mutant FUEL, which stands for folate utilization enzyme for leucovorin, is hypersusceptible to antifolates and unable to metabolize folinic acid. FUEL lacks 5,10-methenyltetrahydrofolate synthase MTHFS activity responsible for the only ATP-dependent, irreversible conversion of folinic acid to 5,10-methenyltetrahydrofolate. In trans expression of active MTHFS proteins from bacteria or human restores both antifolate resistance and folinic acid utilization to FUEL. Absence of MTHFS results in marked cellular accumulation of polyglutamylated species of folinic acid. MTHFS also affects Mycobacterium smegmatis utilization of monoglutamylated 5-methyltetrahydrofolate exogenously added to the medium |
Mycolicibacterium smegmatis |