Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 7,8-dihydropteroate + L-Glu
?
-
Substrates: enzyme of 5,6,7,8-tetrahydropteroyl-Glun synthesis pathway
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
ATP + 7,8-dihydropteroate + L-glutamate
ADP + phosphate + 7,8-dihydropteroylglutamate
ATP + L-glutamate + 7,8-dihydropteroate
ADP + phosphate + 7,8-dihydropteroylglutamate
-
Substrates: assay at pH 10, 37°C
Products: -
?
dATP + 7,8-dihydropteroate + L-Glu
dADP + phosphate + 7,8-dihydrofolate
-
Substrates: 40.5% of the activity relative to ATP
Products: -
?
GTP + 7,8-dihydropteroate + L-Glu
GDP + phosphate + 7,8-dihydrofolate
ITP + 7,8-dihydropteroate + L-Glu
IDP + phosphate + 7,8-dihydrofolate
UTP + 7,8-dihydropteroate + L-Glu
UDP + phosphate + 7,8-dihydrofolate
-
Substrates: 79.8% of the activity relative to ATP
Products: -
?
additional information
?
-
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
Q8W041
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
Serratia indica
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-Glu
ADP + phosphate + 7,8-dihydrofolate
-
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-glutamate
ADP + phosphate + 7,8-dihydropteroylglutamate
-
Substrates: ATP in form of MgATP2-
Products: -
?
ATP + 7,8-dihydropteroate + L-glutamate
ADP + phosphate + 7,8-dihydropteroylglutamate
-
Substrates: ATP in form of MgATP2-
Products: -
?
ATP + 7,8-dihydropteroate + L-glutamate
ADP + phosphate + 7,8-dihydropteroylglutamate
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-glutamate
ADP + phosphate + 7,8-dihydropteroylglutamate
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-glutamate
ADP + phosphate + 7,8-dihydropteroylglutamate
Substrates: -
Products: -
?
ATP + 7,8-dihydropteroate + L-glutamate
ADP + phosphate + 7,8-dihydropteroylglutamate
Substrates: the enzyme is involved in the essential biosynthesis of folates
Products: -
?
ATP + 7,8-dihydropteroate + L-glutamate
ADP + phosphate + 7,8-dihydropteroylglutamate
Substrates: i.e. 7,8-dihydropteroate
Products: -
?
ATP + 7,8-dihydropteroate + L-glutamate
ADP + phosphate + 7,8-dihydropteroylglutamate
Substrates: i.e. 7,8-dihydropteroate
Products: -
?
GTP + 7,8-dihydropteroate + L-Glu
GDP + phosphate + 7,8-dihydrofolate
-
Substrates: 11.0% of the activity relative to ATP
Products: -
?
GTP + 7,8-dihydropteroate + L-Glu
GDP + phosphate + 7,8-dihydrofolate
-
Substrates: 35% of the activity relative to ATP
Products: -
?
GTP + 7,8-dihydropteroate + L-Glu
GDP + phosphate + 7,8-dihydrofolate
Serratia indica
-
Substrates: 37% of the activity relative to ATP
Products: -
?
ITP + 7,8-dihydropteroate + L-Glu
IDP + phosphate + 7,8-dihydrofolate
-
Substrates: 7.8% of the activity relative to ATP
Products: -
?
ITP + 7,8-dihydropteroate + L-Glu
IDP + phosphate + 7,8-dihydrofolate
-
Substrates: at 60% of the activity relative to ATP
Products: -
?
ITP + 7,8-dihydropteroate + L-Glu
IDP + phosphate + 7,8-dihydrofolate
Serratia indica
-
Substrates: 59% of the activity relative to ATP
Products: -
?
additional information
?
-
Substrates: the expression of the enzyme in Escherichia coli and Saccharomyces cerevisiae defective strains restores Escherichia coli cells to methionine and glycine prototrophy on minimal medium, but cannot entirely compensate for the loss of the native homologue in Saccharomyces cerevisiae. The malarial gene encodes a protein carrying dihydrofolate synthetase and folylpolyglutamate synthetase activities, both needed for the de novo folate synthesis
Products: -
?
additional information
?
-
-
Substrates: the expression of the enzyme in Escherichia coli and Saccharomyces cerevisiae defective strains restores Escherichia coli cells to methionine and glycine prototrophy on minimal medium, but cannot entirely compensate for the loss of the native homologue in Saccharomyces cerevisiae. The malarial gene encodes a protein carrying dihydrofolate synthetase and folylpolyglutamate synthetase activities, both needed for the de novo folate synthesis
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
-
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
-
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
-
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)
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)
-
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
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
-
additional information
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
D112A
naturally occuring mutation
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
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
F152L
naturally occuring conserved mutation
F152S
naturally occuring conserved mutation
F461F
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
G111S
naturally occuring mutation
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
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
I43V
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
N73S
naturally occuring conserved mutation
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
R49G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
S150R
naturally occuring conserved mutation
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
-
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
-
D384A
-
naturally occuring mutation in enzyme FolC in clinical isolates of drug-susceptible Mycobacterium tuberculosis
-
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
-
E153A
-
naturally occuring conserved mutation, the mutant shows reduced enzyme activity
-
E153G
-
naturally occuring conserved mutation
-
R410W
-
naturally occuring mutation
-
S150R
-
naturally occuring conserved mutation
-
A183P
naturally occuring conserved mutation, the mutant shows reduced enzyme activity
R49W
naturally occuring conserved mutation, the mutant shows reduced enzyme activity
E153A
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 conserved mutation
E153G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
E40G
naturally occuring mutation
E40G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
I43A
naturally occuring mutation
I43A
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
I43T
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
R410W
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
S150G
naturally occuring conserved mutation
S150G
naturally occuring mutation in enzyme FolC in clinical isolates of drug-resistant Mycobacterium tuberculosis
additional information
4-aminosalicylic acid susceptibility of mutant strains, overview
additional information
-
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
-
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
-
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
-
4-aminosalicylic acid susceptibility of mutant strains, overview
-
additional information
removal of the first 16 or 40 residues of the protein does not abolish the enzyme activity
additional information
-
removal of the first 16 or 40 residues of the protein does not abolish the enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bognar, A.L.; Shane, B.
Bacterial folylpoly(gamma-glutamate) synthase-dihydrofolate synthase
Methods Enzymol.
122
349-359
1986
Corynebacterium sp.
brenda
Bognar, A.L.; Osborne, C.; Shane, B.; Singer, S.C.; Ferone, R.
Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase. Cloning and high expression of the Escherichia coli folC gene and purification and properties of the gene product
J. Biol. Chem.
260
5625-5630
1985
Escherichia coli
brenda
Pongsamart, S.; Ho, R.I.; Corman, L.; Foye, W.O.
Characterization and inhibition of dihydrofolate synthetase from Neisseria gonorrhoeae
Mol. Cell. Biochem.
59
165-171
1984
Neisseria gonorrhoeae
brenda
Shane, B.
Properties of Corynebacterium species dihydrofolate synthetase-folylpolyglutamate synthetase
Chem. Biol. Pteridines, Proc. Int. Symp. Pteridines Folic Acid Deriv. Chem. Biol. Clin. Aspects
621-626
1983
Corynebacterium sp.
-
brenda
Shane, B.; Cichowicz, D.J.
Folylpoly-gamma-glutamate synthetases: properties and regulation
Adv. Exp. Med. Biol.
163
149-165
1983
Corynebacterium sp.
brenda
Ferone, R.; Warskow, A.
Co-purification of dihydrofolate synthetase and N-10formyltetrahydropteroyldiglutamate synthetase from E. coli
Adv. Exp. Med. Biol.
163
167-181
1983
Escherichia coli
brenda
Pongsamart, S.; Ho, R.I.; Corman, L.; Foye, W.O.
Inhibition of dihydrofolate synthetase from Neisseria gonorrhoeae by dihydropteroate and dihydrofolate derivatives
Chem. Biol. Interact.
36
369-373
1981
Neisseria gonorrhoeae
brenda
Iwai, K.; Ikeda, M.; Kobashi, M.
Intracellular distribution, purification, and properties of dihydrofolate synthetase from pea seedlings
Methods Enzymol.
66
581-585
1980
Pisum sativum
brenda
Ho, R.I.
A simple radioassay for dihydrofolate synthetase activity in Escherichia coli and its application to an inhibition study of new pteroate analogs
Methods Enzymol.
66
576-581
1980
Escherichia coli
brenda
Roland, S.; Ferone, R.; Harvey, R.J.; Styles, V.L.; Morrison, R.W.
The characteristics and significance of sulfonamides as substrates for Escherichia coli dihydropteroate synthase
J. Biol. Chem.
254
10337-10345
1979
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Ikeda, M.; Iwai, K.
Some characteristics of the dihydrofolate synthetase from Serratia indica
J. Nutr. Sci. Vitaminol.
22
365-373
1976
Serratia indica
brenda
Ikeda, M.; Iwai, K.
Purification and properties of the dihydrofolate synthetase from Serratia indica
J. Nutr. Sci. Vitaminol.
22
235-248
1976
Serratia indica
brenda
Ho, R.I.; Corman, L.; Ho, J.; Nair, M.G.
A simple radioassay for dihydrofolate synthetase activity in Escherichia coli and its applicationto an inhibition study of new pteroate analogs
Anal. Biochem.
73
493-500
1976
Escherichia coli, Neisseria meningitidis
brenda
Webb, S.R.; Ferone, R.
Inhibition of dihydrofolate synthetase by folate, homofolate, pteroate and homopteroate and their reduced forms
Biochim. Biophys. Acta
422
419-426
1976
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Iwai, K.; Ikeda, M.
Purification and properties of the dihydrofolate synthetase from pea seedlings
J. Nutr. Sci. Vitaminol.
21
7-18
1975
Pisum sativum
brenda
Ikeda, M.; Iwai, K.
The intracellular localization and stability of the dihydrofolate synthetase in pea seedlings
J. Nutr. Sci. Vitaminol.
21
1-6
1975
Pisum sativum, Spinacia oleracea
brenda
Brown, G.M.
Dihydrofolate synthetase
Methods Enzymol.
18B
771-775
1971
Escherichia coli
-
brenda
Shiota, T.; Baugh, C.M.; Jackson, R.; Dillard, R.
The enzymatic synthesis of hydroxymethyldihydropteridine pyrophosphate and dihydrofolate
Biochemistry
8
5022-5028
1969
Lactiplantibacillus plantarum
brenda
Griffin, M.J.; Brown, G.M.
The biosynthesis of folic acid. III. Enzymatic formation of dihydrofolic acid from dihydropteroic acid and of tetrahydropteroylpolyglutamic acid compounds from tetrahydrofolic acid
J. Biol. Chem.
239
310-316
1964
Priestia megaterium, Saccharomyces cerevisiae, Corynebacterium sp., Escherichia coli, Enterococcus faecalis, Mycobacterium avium, Mycolicibacterium phlei, Neurospora crassa
brenda
Lacks, S.A.; Greenberg, B.; Lopez, P.
A cluster of four genes encoding enzymes for five steps in the folate biosynthetic pathway of Streptococcus pneumoniae
J. Bacteriol.
177
66-74
1995
Streptococcus pneumoniae
brenda
Fussenegger, M.; Meyer, T.F.
Cloning and characterization of the Neisseria gonorrhoeae MS11 folC gene
Mol. Gen. Genet.
250
277-285
1996
Neisseria gonorrhoeae
brenda
Neuburger, M.; Rebeille, F.; Jourdain, A.; Nakamura, S.; Douce, R.
Mitochondia are a major site for folate and thymidylate syntheis in plants
J. Biol. Chem.
271
9466-9472
1996
Pisum sativum
brenda
Patel, O.; Castelli, L.; Fernley, R.; Coloe, P.; Macreadie, I.
Production of a functional dihydrofolate synthase with a cleavable poly-His tag in Saccharomyces cerevisiae
Biotechnol. Lett.
24
657-662
2002
Saccharomyces cerevisiae, Saccharomyces cerevisiae CUY13
brenda
Salcedo, E.; Cortese, J.F.; Plowe, C.V.; Sims, P.F.G.; Hyde, J.E.
A bifunctional dihydrofolate synthetase--folylpolyglutamate synthetase in Plasmodium falciparum identified by functional complementation in yeast and bacteria
Mol. Biochem. Parasitol.
112
239-252
2001
Plasmodium falciparum (Q9U738), Plasmodium falciparum
brenda
Ravanel, S.; Cherest, H.; Jabrin, S.; Grunwald, D.; Surdin-Kerjan, Y.; Douce, R.; Rebeille, F.
Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
98
15360-15365
2001
Arabidopsis thaliana (Q8W041), Arabidopsis thaliana
brenda
Mathieu, M.; Debousker, G.; Vincent, S.; Viviani, F.; Bamas-Jacques, N.; Mikol, V.
Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy
J. Biol. Chem.
280
18916-18922
2005
Escherichia coli
brenda
Levin, I.; Giladi, M.; Altman-Price, N.; Ortenberg, R.; Mevarech, M.
An alternative pathway for reduced folate biosynthesis in bacteria and halophilic archaea
Mol. Microbiol.
54
1307-1318
2004
Haloarcula marismortui, Halobacterium salinarum, Haloferax volcanii
brenda
Hauser, P.M.; Macreadie, I.G.
Isolation of the Pneumocystis carinii dihydrofolate synthase gene and functional complementation in Saccharomyces cerevisiae
FEMS Microbiol. Lett.
256
244-250
2006
Pneumocystis carinii (Q2VIK1), Pneumocystis carinii
brenda
Wang, P.; Wang, Q.; Yang, Y.; Coward, J.K.; Nzila, A.; Sims, P.F.; Hyde, J.E.
Characterisation of the bifunctional dihydrofolate synthase-folylpolyglutamate synthase from Plasmodium falciparum; a potential novel target for antimalarial antifolate inhibition
Mol. Biochem. Parasitol.
172
41-51
2010
Plasmodium falciparum
brenda
Bacon, D.; Tang, D.; Salas, C.; Roncal, N.; Lucas, C.; Gerena, L.; Tapia, L.; Llanos-Cuentas, A.; Garcia, C.; Solari, L.; Kyle, D.; Magill, A.
Effects of point mutations in Plasmodium falciparum dihydrofolate reductase and dihydropterate synthase genes on clinical outcomes and in vitro susceptibility to sulfadoxine and pyrimethamine
PLoS ONE
4
e6762
2009
Plasmodium falciparum
brenda
Zhao, F.; Wang, X.D.; Erber, L.N.; Luo, M.; Guo, A.Z.; Yang, S.S.; Gu, J.; Turman, B.J.; Gao, Y.R.; Li, D.F.; Cui, Z.Q.; Zhang, Z.P.; Bi, L.J.; Baughn, A.D.; Zhang, X.E.; Deng, J.Y.
Binding pocket alterations in dihydrofolate synthase confer resistance to para-aminosalicylic acid in clinical isolates of Mycobacterium tuberculosis
Antimicrob. Agents Chemother.
58
1479-1487
2014
Mycobacterium tuberculosis (I6Y0R5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (I6Y0R5), Mycobacterium tuberculosis variant bovis (A0A0H3M8P3), Mycobacterium tuberculosis variant bovis
brenda
Luraschi, A.; Cisse, O.H.; Monod, M.; Pagni, M.; Hauser, P.M.
Functional characterization of the Pneumocystis jirovecii potential drug targets dhfs and abz2 involved in folate biosynthesis
Antimicrob. Agents Chemother.
59
2560-2566
2015
Pneumocystis jirovecii (L0PF87), Pneumocystis jirovecii, Pneumocystis jirovecii SE8 (L0PF87)
brenda
Cheng, V.W.; Leung, K.S.; Kwok, J.S.; Leung, R.K.; Yang, K.Y.; Chan, R.C.; Kam, K.M.; Tsui, S.K.
Phylogenetic and structural significance of dihydrofolate synthase (folC) mutations in drug-resistant Mycobacterium tuberculosis
Microb. Drug Resist.
22
545-551
2016
Mycobacterium tuberculosis (I6Y0R5), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 / H37Rv (I6Y0R5)
brenda