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
Advanced search results
Engineering
Engineering on EC 6.3.2.12 - dihydrofolate synthase
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A132E
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
A171A
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
A420V
naturally occuring mutation in enzyme FolC in clinical isolates of both drug-resistant and drug-susceptible Mycobacterium tuberculosis
A457V
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
D111A
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
D135A
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
D324G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
D384A
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
E153A
E153G
E40G
E40K
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
E434Q
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
F461F
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
G112S
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
G284G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
G422G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
I43A
I43F
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
I43S
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
I43T
I43V
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
P21L
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
P356L
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
P8P
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
P9P
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
R268R
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
R410W
R49G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
S150G
S335I
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
V256A
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
D111A
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
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D384A
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
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E153A
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
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E153G
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
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E153A
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naturally occuring conserved mutation, the mutant shows reduced enzyme activity
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A183P
naturally occuring conserved mutation, the mutant shows reduced enzyme activity
R49W
naturally occuring conserved mutation, the mutant shows reduced enzyme activity
additional information
naturally occuring conserved mutation, the mutant shows reduced enzyme activity
E153A
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
E153G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
E40G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
I43A
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
naturally occuring mutation, the mutant shows reduced enzyme activity
I43T
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
R410W
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
S150G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
4-aminosalicylic acid susceptibility of mutant strains, overview
additional information
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4-aminosalicylic acid susceptibility of mutant strains, overview
additional information
phylogenetic and structural significance of mutations in gene folC in drug-resistant Mycobacterium tuberculosis, overview. Genotyping of 254 clinical isolates. Enzyme residues E40, I43, S150, and E153 are the most frequently affected amino acid residues in resistant isolates with mutant enzymes, distribution of mutations in the genome-based phylogenetic tree, overview. Mutations at E40, I43, and S150 can alter the structure of the FolC putative binding pocket, causing the PAS derivative to bind outside of the then deformed pocket
additional information
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phylogenetic and structural significance of mutations in gene folC in drug-resistant Mycobacterium tuberculosis, overview. Genotyping of 254 clinical isolates. Enzyme residues E40, I43, S150, and E153 are the most frequently affected amino acid residues in resistant isolates with mutant enzymes, distribution of mutations in the genome-based phylogenetic tree, overview. Mutations at E40, I43, and S150 can alter the structure of the FolC putative binding pocket, causing the PAS derivative to bind outside of the then deformed pocket
additional information
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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phylogenetic and structural significance of mutations in gene folC in drug-resistant Mycobacterium tuberculosis, overview. Genotyping of 254 clinical isolates. Enzyme residues E40, I43, S150, and E153 are the most frequently affected amino acid residues in resistant isolates with mutant enzymes, distribution of mutations in the genome-based phylogenetic tree, overview. Mutations at E40, I43, and S150 can alter the structure of the FolC putative binding pocket, causing the PAS derivative to bind outside of the then deformed pocket
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additional information
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4-aminosalicylic acid susceptibility of mutant strains, overview
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additional information
removal of the first 16 or 40 residues of the protein does not abolish the enzyme activity
additional information
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removal of the first 16 or 40 residues of the protein does not abolish the enzyme activity