EC Number   |
General Information |
Reference |
|---|
    6.3.2.12 | malfunction |
in Mycobacterium bovis clinical isolates missense mutations within the coding sequence of the folC gene cause alterations within the 7,8-dihydropteroate binding pocket resulting in 4-aminosalicylic acid resistance. The alterations in the substrate binding pocket result in reduced dihydrofolate synthase activity and abolish the bioactivation of hydroxydihydropteroate to hydroxydihydrofolate. Introduction of a wild-type copy of folC fully restores PAS susceptibility in folC mutant strains |
726690 |
| 6.3.2.12 | malfunction |
in Mycobacterium tuberculosis clinical isolates missense mutations within the coding sequence of the folC gene cause alterations within the 7,8-dihydropteroate binding pocket resulting in 4-aminosalicylic acid resistance. The alterations in the substrate binding pocket result in reduced dihydrofolate synthase activity and abolish the bioactivation of hydroxydihydropteroate to hydroxydihydrofolate. Introduction of a wild-type copy of folC fully restores PAS susceptibility in folC mutant strains |
-, 726690 |
| 6.3.2.12 | malfunction |
mutations at residues E40, I43, and S150 can alter the structure of FolC's putative binding pocket, causing the PAS derivative to bind outside of the then deformed pocket |
-, 745706 |
| 6.3.2.12 | metabolism |
the enzyme is involved in the biosynthesis of folic acid and tetrahydrofolate, pathway overview. The DHFS enzyme carries out the final step of folic acid biosynthesis, namely, the addition of a glutamate to dihydropteroate to make folic acid (i.e. dihydrofolate) |
-, 744052 |
| 6.3.2.12 | more |
homology modeling of wild-type and mutated FolC, docking study using hydroxydihydropteroate, the metabolic derivative of para-aminosalicylic acid (PAS), to evaluate the binding affinity changes. Para-aminosalicylic acid (PAS) is an example of an anti-tuberculosis agent that blocks the folate pathway in Mycobacterium tuberculosis |
-, 745706 |
| 6.3.2.12 | physiological function |
the enzyme is essential for the life of the pathogen. The enzyme catalyzes the last step of folic acid, i.e. vitamin B9, biosynthesis |
-, 744052 |
