6.3.2.12: dihydrofolate synthase
This is an abbreviated version!
For detailed information about dihydrofolate synthase, go to the full flat file.
Word Map on EC 6.3.2.12
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6.3.2.12
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tetrahydrofolate
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polyglutamylated
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analysis
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medicine
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drug development
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biotechnology
- 6.3.2.12
- tetrahydrofolate
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polyglutamylated
- analysis
- medicine
- drug development
- biotechnology
Reaction
Synonyms
7,8-Dihydrofolate synthetase, 7,8-Dihydropteroate:L-glutamate ligase (ADP), DHFR, DHFS, dihydrofolate reductase, dihydrofolate synthase, Dihydrofolate synthetase, dihydrofolate synthetase-folylpolyglutamate synthetase, dihydropteroate:L-glutamate ligase (ADP-forming), FHFS, FHFS/FPGS, FolC, Folylpoly-(gamma-glutamate) synthetase-dihydrofolate synthase, Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase, H2-folate synthetase, LH57_13380, PfDHFS-FPGS, PNEJI1_000945, Rv2447c, Synthetase, dihydrofolate
ECTree
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General Information
General Information on EC 6.3.2.12 - dihydrofolate synthase
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malfunction
metabolism
physiological function
additional information
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
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
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
malfunction
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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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
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malfunction
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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
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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)
metabolism
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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)
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the enzyme is essential for the life of the pathogen. The enzyme catalyzes the last step of folic acid, i.e. vitamin B9, biosynthesis
physiological function
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the enzyme is essential for the life of the pathogen. The enzyme catalyzes the last step of folic acid, i.e. vitamin B9, biosynthesis
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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
additional information
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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
additional information
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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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
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