Any feedback?
Literature summary extracted from
- 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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
