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(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
7,8-dihydropteroate + diphosphate
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + 4-aminobenzoate
7,8-dihydropteroate + diphosphate
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoylglutamate
diphosphate + dihydrofolate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + sulfamethoxazole
diphosphate + dihydropterin-sulfamethoxazole
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + sulfanilamide
diphosphate + dihydropterin-sulfanilamide
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + sulfathiazole
diphosphate + dihydropterin-sulfathiazole
4-aminobenzoate + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
diphosphate + 7,8-dihydropteroate
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
dapson + Mg-6-hydroxymethyl-7,8-dihydropterin diphosphate
diphosphate + 2-amino-6-[([4-[(4-aminophenyl)sulfonyl]phenyl]amino)methyl]-7,8-dihydropteridin-4(3H)-one
-
-
-
?
p-aminobenzoate + 6-hydroxymethyl-7,8-dihydropterin-diphosphate
diphosphate + 7,8-dihydropteroate
p-aminobenzoic acid + 6-hydroxymethyl-7,8-dihydropterin diphosphate
diphosphate + 7,8-dihydropteroate
substrate binding order: 6-hydroxymethyl-7,8-dihydropterin diphosphate binds prior to p-aminobenzoic acid, 6-hydroxymethyl-7,8-dihydropterin diphosphate binding with KD: 33 +/-6 microM (k(on): 260000 1/M*s, k(off): 8.7 1/s) as revealed by fluorescence spectroscopy, p-aminobenzoic acid binding to diphosphate-enzyme complex: KD: 0.13 +/-0.02 microM
diphosphate-binding allows binding of p-aminobenzoic acid or p-aminobenzoic acid analogues, diphosphate binding with KD: 350 +/-20 microM (k(on): 56000 1/M*s, k(off): 21 1/s) as revealed by fluorescence spectroscopy
-
?
sulfadiazine + 6-hydroxymethyl-7,8-dihydropterin diphosphate
diphosphate + 4-[[(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)methyl]amino]-N-pyrimidin-2-ylbenzenesulfonamide
-
-
-
?
sulfamethizole + 6-hydroxymethyl-7,8-dihydropterin diphosphate
?
-
-
-
?
sulfamethizole + 6-hydroxymethyl-7,8-dihydropterin diphosphate
diphosphate + 4-[[(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)methyl]amino]-N-(5-methyl-1,3,4-thiadiazol-2-yl)benzenesulfonamide
-
-
-
?
sulfamethoxazole + 6-hydroxymethyl-7,8-dihydropterin diphosphate
diphosphate + 4-[[(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)methyl]amino]-N-(5-methylisoxazol-3-yl)benzenesulfonamide
-
-
-
?
sulfanilamide + 6-hydroxymethyl-7,8-dihydropterin diphosphate
diphosphate + 4-[[(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)methyl]amino]benzenesulfonamide
-
-
-
?
sulfathiazole + 6-hydroxymethyl-7,8-dihydropterin diphosphate
diphosphate + 4-[[(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)methyl]amino]-N-1,3-thiazol-2-ylbenzenesulfonamide
-
-
-
?
sulfisoxazole + 6-hydroxymethyl-7,8-dihydropterin diphosphate
?
-
-
-
?
additional information
?
-
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
7,8-dihydropteroate binding mode, overview
-
r
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
the enzyme catalyzes the condensation between (7,8-dihydropterin-6-yl)methyl diphosphate and 4-aminobenzoate to produce 7,8-dihydropteroate, a precursor of tetrahydrofolate. It plays a great role in folate synthesis pathway essential for amino acids biosynthesis
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
the enzyme catalyzes the condensation between (7,8-dihydropterin-6-yl)methyl diphosphate and 4-aminobenzoate to produce 7,8-dihydropteroate, a precursor of tetrahydrofolate. It plays a great role in folate synthesis pathway essential for amino acids biosynthesis
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
A0A384KP04
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
A0A384KP04
the enzyme catalyzes the condensation between (7,8-dihydropterin-6-yl)methyl diphosphate and 4-aminobenzoate to produce 7,8-dihydropteroate, a precursor of tetrahydrofolate. It plays a great role in folate synthesis pathway essential for amino acids biosynthesis
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
A0A384KP04
mechanistic proposals for dihydropteroate synthase have been systematically investigated using a hybrid QM/MM method. A reaction mechanism is proposed that follows an SN1 process with the rate determining step being C-O bond breaking to give a carbocation intermediate
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
A0A384KP04
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + 4-aminobenzoate
7,8-dihydropteroate + diphosphate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + 4-aminobenzoate
7,8-dihydropteroate + diphosphate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + sulfamethoxazole
diphosphate + dihydropterin-sulfamethoxazole
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + sulfamethoxazole
diphosphate + dihydropterin-sulfamethoxazole
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + sulfathiazole
diphosphate + dihydropterin-sulfathiazole
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + sulfathiazole
diphosphate + dihydropterin-sulfathiazole
-
-
-
?
4-aminobenzoate + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
diphosphate + 7,8-dihydropteroate
-
-
-
?
4-aminobenzoate + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
diphosphate + 7,8-dihydropteroate
-
-
-
?
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
pH 7.5, folate biosynthesis
coupled with diphosphate-dependent phosphofructokinase, aldolase, triosephosphate isomerase, alpha-glycerophosphate dehydrogenase, in presence of NADH and D-fructose 6-phosphate, decrease in NADH monitored as change of absorbance at 340 nm
-
?
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
p-aminobenzoate + 6-hydroxymethyl-7,8-dihydropterin-diphosphate
diphosphate + 7,8-dihydropteroate
5 mM MgCl2, 1 mM dithiothreitol, 37°C, pH 7-9.5
-
-
?
p-aminobenzoate + 6-hydroxymethyl-7,8-dihydropterin-diphosphate
diphosphate + 7,8-dihydropteroate
5 mM MgCl2, 1 mM dithiothreitol, 37°C, pH 7-9.5
-
-
?
additional information
?
-
-
the enzyme is bifunctional exhibiting 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK, and dihydropteroate synthase, DHPS, activities
-
-
?
additional information
?
-
binding of 6-hydroxymethyl-7,8-dihydropterin-diphosphate with KD: 117 microM, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of 6-hydroxymethyl-7,8-dihydropterin-diphosphate with KD: 117 microM, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
-
binding of 6-hydroxymethyl-7,8-dihydropterin-diphosphate with KD: 117 microM, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of 6-hydroxymethyl-7,8-dihydropterin-diphosphate with KD: 4.6 microM, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of 6-hydroxymethyl-7,8-dihydropterin-diphosphate with KD: 4.6 microM, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
-
binding of 6-hydroxymethyl-7,8-dihydropterin-diphosphate with KD: 4.6 microM, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of dapsone (p-aminobenzoate substrate analog) with KD: 168 microM, in absence of 6-hydroxymethyl-7,8-dihydropterin-diphosphate, , revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of dapsone (p-aminobenzoate substrate analog) with KD: 168 microM, in absence of 6-hydroxymethyl-7,8-dihydropterin-diphosphate, , revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
-
binding of dapsone (p-aminobenzoate substrate analog) with KD: 168 microM, in absence of 6-hydroxymethyl-7,8-dihydropterin-diphosphate, , revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of dapsone (p-aminobenzoate substrate analog) with KD: 96 microM, in absence of 6-hydroxymethyl-7,8-dihydropterin-diphosphate, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of dapsone (p-aminobenzoate substrate analog) with KD: 96 microM, in absence of 6-hydroxymethyl-7,8-dihydropterin-diphosphate, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
-
binding of dapsone (p-aminobenzoate substrate analog) with KD: 96 microM, in absence of 6-hydroxymethyl-7,8-dihydropterin-diphosphate, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
Rv1207 lacks dihydropteroate synthase activity in presence of 10 microM p-aminobenzoate and 10 microM 6-hydroxymethyl-7,8-dihydropterin-diphosphate, 5 mM MgCl2, 1 mM dithiothreitol, 37°C, pH 7-9.5
-
-
?
additional information
?
-
Rv1207 lacks dihydropteroate synthase activity in presence of 10 microM p-aminobenzoate and 10 microM 6-hydroxymethyl-7,8-dihydropterin-diphosphate, 5 mM MgCl2, 1 mM dithiothreitol, 37°C, pH 7-9.5
-
-
?
additional information
?
-
-
Rv1207 lacks dihydropteroate synthase activity in presence of 10 microM p-aminobenzoate and 10 microM 6-hydroxymethyl-7,8-dihydropterin-diphosphate, 5 mM MgCl2, 1 mM dithiothreitol, 37°C, pH 7-9.5
-
-
?
additional information
?
-
binding of 6-hydroxymethyl-7,8-dihydropterin-diphosphate with KD: 117 microM, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of 6-hydroxymethyl-7,8-dihydropterin-diphosphate with KD: 117 microM, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of dapsone (p-aminobenzoate substrate analog) with KD: 96 microM, in absence of 6-hydroxymethyl-7,8-dihydropterin-diphosphate, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of dapsone (p-aminobenzoate substrate analog) with KD: 96 microM, in absence of 6-hydroxymethyl-7,8-dihydropterin-diphosphate, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
Rv1207 lacks dihydropteroate synthase activity in presence of 10 microM p-aminobenzoate and 10 microM 6-hydroxymethyl-7,8-dihydropterin-diphosphate, 5 mM MgCl2, 1 mM dithiothreitol, 37°C, pH 7-9.5
-
-
?
additional information
?
-
Rv1207 lacks dihydropteroate synthase activity in presence of 10 microM p-aminobenzoate and 10 microM 6-hydroxymethyl-7,8-dihydropterin-diphosphate, 5 mM MgCl2, 1 mM dithiothreitol, 37°C, pH 7-9.5
-
-
?
additional information
?
-
binding of 6-hydroxymethyl-7,8-dihydropterin-diphosphate with KD: 4.6 microM, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of 6-hydroxymethyl-7,8-dihydropterin-diphosphate with KD: 4.6 microM, revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of dapsone (p-aminobenzoate substrate analog) with KD: 168 microM, in absence of 6-hydroxymethyl-7,8-dihydropterin-diphosphate, , revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
binding of dapsone (p-aminobenzoate substrate analog) with KD: 168 microM, in absence of 6-hydroxymethyl-7,8-dihydropterin-diphosphate, , revealed by fluorescence spectroscopy
-
-
?
additional information
?
-
-
amino acid V585 may be responsible for resistance of Plasmodium vivax to sulfadoxine
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-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
7,8-dihydropteroate + diphosphate
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoylglutamate
diphosphate + dihydrofolate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + sulfamethoxazole
diphosphate + dihydropterin-sulfamethoxazole
4-aminobenzoate + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
diphosphate + 7,8-dihydropteroate
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
additional information
?
-
-
amino acid V585 may be responsible for resistance of Plasmodium vivax to sulfadoxine
-
-
?
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
r
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
the enzyme catalyzes the condensation between (7,8-dihydropterin-6-yl)methyl diphosphate and 4-aminobenzoate to produce 7,8-dihydropteroate, a precursor of tetrahydrofolate. It plays a great role in folate synthesis pathway essential for amino acids biosynthesis
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
the enzyme catalyzes the condensation between (7,8-dihydropterin-6-yl)methyl diphosphate and 4-aminobenzoate to produce 7,8-dihydropteroate, a precursor of tetrahydrofolate. It plays a great role in folate synthesis pathway essential for amino acids biosynthesis
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
A0A384KP04
-
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
A0A384KP04
the enzyme catalyzes the condensation between (7,8-dihydropterin-6-yl)methyl diphosphate and 4-aminobenzoate to produce 7,8-dihydropteroate, a precursor of tetrahydrofolate. It plays a great role in folate synthesis pathway essential for amino acids biosynthesis
-
-
?
(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
A0A384KP04
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + sulfamethoxazole
diphosphate + dihydropterin-sulfamethoxazole
-
-
-
?
2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + sulfamethoxazole
diphosphate + dihydropterin-sulfamethoxazole
-
-
-
?
4-aminobenzoate + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
diphosphate + 7,8-dihydropteroate
-
-
-
?
4-aminobenzoate + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate
diphosphate + 7,8-dihydropteroate
-
-
-
?
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate
diphosphate + 7,8-dihydropteroate
-
-
-
?
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.
(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)acetic acid
-
-
(7-amino-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)acetic acid
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-(ethylthio)-acrylamide
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-mercapto-acrylamide
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(methylamino)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-mercapto-3-(methylamino)acrylamide
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl) amino]sulfonyl]phenyl)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-galactopyranosylthio)acrylamide
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-galactopyranosylthio)acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylthio)-acrylamide
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N,N-diethylacetamide
-
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N,N-dimethylacetamide
-
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N-(2-methylpropyl)acetamide
-
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N-(3-methylbenzyl)acetamide
-
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N-butylacetamide
-
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N-cyclohexylacetamide
-
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N-cyclopropylacetamide
-
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N-ethyl-N-methylpropanamide
-
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N-methylacetamide
-
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N-phenylacetamide
-
2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)-N-tert-butylacetamide
-
2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoate
-
binding structure, interactions with the DHPS module and the HPPK module, modeling, ovverview
2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
2-(7-amino-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
-
-
2-amino-4-hydroxy-6-hydroxymethyl-dihydropteridine
-
-
2-amino-6-[[4-(4-aminobenzene-1-sulfonyl)anilino]methyl]pteridin-4(1H)-one
-
2-amino-8-(2-hydroxyethyl)-1,9-dihydro-6H-purin-6-one
-
2-amino-8-(2-oxopropyl)-1,9-dihydro-6H-purin-6-one
-
2-amino-8-(3-hydroxypropyl)-1,9-dihydro-6H-purin-6-one
-
2-amino-8-(benzylsulfanyl)-9-methyl-1,9-dihydro-6H-purin-6-one
-
2-amino-8-(methylsulfanyl)-1,9-dihydro-6H-purin-6-one
-
2-amino-8-(morpholin-4-yl)-1,9-dihydro-6H-purin-6-one
-
2-amino-8-(phenylethynyl)-1,9-dihydro-6H-purin-6-one
-
2-amino-8-bromo-1,9-dihydro-6H-purin-6-one
-
2-amino-8-hydroxy-1,9-dihydro-6H-purin-6-one
-
2-amino-8-hydroxy-9-methyl-1,9-dihydro-6H-purin-6-one
-
2-amino-8-methyl-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(2,3-dimethylbenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(2,4-difluorobenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(2,5-dimethylbenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(2-bromobenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(2-chlorobenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(2-fluoro-3-methylbenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(2-fluoro-5-methylbenzyl)sulfanyl]-9-methyl-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(2-fluorobenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(2-methylbenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(2-nitrobenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(3,4-difluorobenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(3,5-dimethylbenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(3-methoxybenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(3-methylbenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(4-fluoro-2-methylbenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(4-fluoro-3-methylbenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(4-fluorobenzyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(naphthalen-1-ylmethyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(naphthalen-2-ylmethyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[(pyridin-4-ylmethyl)sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[2-(4-bromophenyl)-2-oxoethyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[2-(4-methoxyphenyl)-2-oxoethyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[2-(morpholin-4-yl)-2-oxoethyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-8-[[(6,6-difluorocyclohexa-2,4-dien-1-yl)methyl]sulfanyl]-1,9-dihydro-6H-purin-6-one
-
2-amino-9-benzyl-8-sulfanyl-1,9-dihydro-6H-purin-6-one
-
2-amino-9-ethyl-8-sulfanyl-1,9-dihydro-6H-purin-6-one
-
2-amino-9-methyl-1,9-dihydro-6H-purin-6-one
-
2-amino-9-methyl-8-sulfanyl-1,9-dihydro-6H-purin-6-one
-
2-amino-9-phenyl-8-sulfanyl-1,9-dihydro-6H-purin-6-one
-
2-[(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl]-N-(3-chlorobenzyl)acetamide
-
2-[(2-amino-9-methyl-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl]-N-phenylacetamide
-
2-[[(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl]methyl]benzonitrile
-
3-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)butanoic acid
-
-
3-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
-
-
3-(7-amino-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
-
-
3-[[(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl]methyl]benzonitrile
-
4,4-Diaminodiphenyl sulfone
-
-
4-[2-[(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl]ethyl]benzenesulfonamide
-
4-[[(2-amino-4-oxo-1,4-dihydropteridin-6-yl)methyl]amino]-N-(2,6-dimethoxypyrimidin-4-yl)benzene-1-sulfonamide
-
4-[[(2-amino-4-oxo-1,4-dihydropteridin-6-yl)methyl]amino]-N-(3,4-dimethyl-1,2-oxazol-5-yl)benzene-1-sulfonamide
-
4-[[(2-amino-4-oxo-1,4-dihydropteridin-6-yl)methyl]amino]-N-(5,6-dimethoxypyrimidin-4-yl)benzene-1-sulfonamide
-
4-[[(2-amino-4-oxo-1,4-dihydropteridin-6-yl)methyl]amino]-N-(5-methyl-1,2-oxazol-3-yl)benzene-1-sulfonamide
-
4-[[(2-amino-4-oxo-1,4-dihydropteridin-6-yl)methyl]amino]-N-(pyridin-2-yl)benzene-1-sulfonamide
-
4-[[(2-amino-4-oxo-1,4-dihydropteridin-6-yl)methyl]amino]-N-(pyrimidin-2-yl)benzene-1-sulfonamide
-
4-[[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino]-N-(3,4-dimethyl-1,2-oxazol-5-yl)benzene-1-sulfonamide
5-nitro-6-methylamino-isocytosine
-
6-hydroxymethylpterin monophosphate
6HMP, competitive inhibitor, 6-hydroxymethyl-7,8-dihydropterin diphosphate analogue
6-methylamino-5-nitrosoisocytosine
-
7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazine-3-carboxylic acid
-
-
7-amino-3-(1-carboxyethyl)-1-methyl-pyrimido (4,5-c)-pyridazine-4,5(1H,6H)-dione
dapson
KD: 0.2 microM according to molecular modelling
dihydrofolate monoglutamate
-
-
Guanidine HCl
-
0.25 M, 50% inhibition
N-(4-(trifluoromethyl)-benzylidene)-1-(4-(trifluoromethyl))benzylamine
N-(4-[[(2-amino-4-oxo-1,4-dihydropteridin-6-yl)methyl]amino]benzene-1-sulfonyl)acetamide
-
p-aminobenzoylglutamate
-
weak
potassium 4-([(2-amino-4-oxo-3,4-dihydro-pyrido[2,3-d]pyrimidin-6-yl)-(2-phosphonoethyl)-amino]-methyl)-benzoate
-
the oxidized analogue shows significant DHPS inhibition and significant antimicrobial activity
potassium 4-([(2-amino-4-oxo-3,4-dihydro-pyrido[2,3-d]pyrimidin-6-yl)-(3-phosphonopropyl)-amino]-methyl)-benzoate
-
the oxidized analogue shows significant DHPS inhibition and significant antimicrobial activity
Pteroate
inhibition of dihydropteroate synthase activity
Pteroic acid
PTA, product analog, binds pterin- and 4-aminobenzoate-binding regions
sulfadoxine-pyrimethamine
-
sulfamethazine
inhibition of dihydropteroate synthase activity
sulfamonomethoxine
inhibition of dihydropteroate synthase activity
sulfamoxisole
-
effective against wild-type enzyme and mutant enzymes A437G/K540E, A437G, S436F/A437G/A613S and S436F/A437G/A613T. Ineffective against A437G/A581G
-
Sulfonamides
-
act as competitive inhibitors with respect to the 4-amino benzoic acid substrate within the DHPS enzyme active site. The 4-amino benzoic acid/sulfonamide binding site is formed close to the protein surface by flexible protein loops facilitating rapid development of sulfonamide resistance. Study of inhibitors designed to target the conserved central pterin binding site within DHPS, molecular dynamics simulation and molecular modeling, overview. Design and synthesis of transition state analogues with ability to mimic the intermediate transient carbocation by the incorporation of a basic amine at the 6-position of the pterin ring
sulfpyridine
-
effective against wild-type enzyme. Ineffective against mutants A437G, A437G/A581G, A437G/K540E, S436F/A437G/A613S and S436F/A437G/A613T
-
tert-butyl (2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)acetate
-
tert-butyl 2-(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)propanoate
-
tetrahydrofolate monoglutamate
-
-
trimethoprim-sulfamethoxazole
-
Trp-Lys
WK, highly potent with KD: 0.23 nM according to structure-based molecular modelling and docking, overlaps with pterin monophosphate and pteroic acid binding regions, highly selective for microbial DHPS compared to human pterin and folate-binding enzymes (dihydrofolate reductase, thymidylate synthase)
Urea
-
0.9 M, 50% inhibition
[(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl](phenyl)acetic acid
-
[(2-amino-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl]acetic acid
-
[(2-amino-9-methyl-6-oxo-6,9-dihydro-1H-purin-8-yl)sulfanyl]acetic acid
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-(ethylthio)-acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-(ethylthio)-acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-(ethylthio)-acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-(ethylthio)-acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-mercapto-acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-mercapto-acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-mercapto-acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylamino)-3-mercapto-acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(methylamino)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(methylamino)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(methylamino)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(methylamino)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-mercapto-3-(methylamino)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-mercapto-3-(methylamino)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-mercapto-3-(methylamino)acrylamide
-
-
(E)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-mercapto-3-(methylamino)acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl) amino]sulfonyl]phenyl)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-galactopyranosylthio)acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl) amino]sulfonyl]phenyl)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-galactopyranosylthio)acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl) amino]sulfonyl]phenyl)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-galactopyranosylthio)acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosylthio)acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylthio)-acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylthio)-acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylthio)-acrylamide
-
-
(E)-3-(allylamino)-2-cyano-N-(4-[[(3,4-dimethylisoxazol-5-yl)amino]sulfonyl]phenyl)-3-(ethylthio)-acrylamide
-
-
2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
-
-
2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
86% inhibition at 0.25 mM
2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
-
46% inhibition at 0.25 mM
2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
-
61% inhibition at 0.25 mM
4-[[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino]-N-(3,4-dimethyl-1,2-oxazol-5-yl)benzene-1-sulfonamide
drug-resistant strains of Helicobacter pylori and multitudinous drug reactions are obstacles in the treatment of Helicobacter pylori infections a reliable tertiary structure of dihydropteroate synthase in complex with inhibitor 4-[[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino]-N-(3,4-dimethyl-1,2-oxazol-5-yl)benzene-1-sulfonamide is constructed by Modeler 9v19. DrugBank compounds of DHPS, published inhibitors, and co-crystal ligand (4-[[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino]-N-(3,4-dimethyl-1,2-oxazol-5-yl)benzene-1-sulfonamide) are docked against dihydropteroate synthase. The best docked compounds are screened against 28.5 million compounds result 1186 structural analogs. Virtual screening workflow and quantum polarized ligand dockings of these compounds against dihydropteroate synthase result three leads that show better XP Gscores, ADME properties, and binding-free energies compared to 4-[[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino]-N-(3,4-dimethyl-1,2-oxazol-5-yl)benzene-1-sulfonamide, DrugBank compounds, and published inhibitors. The proposed leads are also validated by receiver operative characteristic (ROC) curve metrics in the presence of thousand decoys and the best docked existing compounds against DHPS. Long-range molecular dynamics (MD) simulations for 100 ns are executed after post-docking evaluations. Trajectory analysis shows that inter-molecular interactions of the lead-dihydropteroate synthase docking complex are stable throughout the entire runtime of MD simulations than 6MB-DHPS complex and Eliglustat-DHPS complex. The study outcomes showed good competitive binding propensity and active-tunneling of leads over the existing inhibitors, thereby these leads could be ideal inhibitors against dihydropteroate synthase to target Helicobacter pylori
4-[[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino]-N-(3,4-dimethyl-1,2-oxazol-5-yl)benzene-1-sulfonamide
A0A384KP04
-
7,8-Dihydropteroic acid
-
-
7,8-Dihydropteroic acid
-
-
7-amino-3-(1-carboxyethyl)-1-methyl-pyrimido (4,5-c)-pyridazine-4,5(1H,6H)-dione
-
-
7-amino-3-(1-carboxyethyl)-1-methyl-pyrimido (4,5-c)-pyridazine-4,5(1H,6H)-dione
-
-
dapsone
-
dapsone
-
effective against wild-type enzyme and mutants A437G/K540E and A437G. Ineffective against mutants A437G/A581G, S436F/A437G/A613S and S436F/A437G/A613T
dapsone
inhibition of dihydropteroate synthase activity
dihydrofolate
-
-
N-(4-(trifluoromethyl)-benzylidene)-1-(4-(trifluoromethyl))benzylamine
complete inhibition at 0.25 mM
N-(4-(trifluoromethyl)-benzylidene)-1-(4-(trifluoromethyl))benzylamine
-
complete inhibition at 0.25 mM
N-(4-(trifluoromethyl)-benzylidene)-1-(4-(trifluoromethyl))benzylamine
-
complete inhibition at 0.25 mM
p-Aminosalicylate
-
p-Aminosalicylic acid
-
-
p-Aminosalicylic acid
-
-
phosphanilic acid
-
28% inhibition at 2.0 mM, complete inhibition at 20 mM
phosphanilic acid
-
22% inhibition at 2.0 mM, 84% inhibition at 20 mM
pyrimethamine
-
-
sulfacetamide
-
competitive inhibitor
sulfacetamide
-
effective against wild-type enzyme and mutant enzymes A437G/K540E, A437G, A437G/A581G, S436F/A437G/A613S and S436F/A437G/A613T
sulfacetamide
-
competitive inhibitor
sulfachloropyridazine
-
effective against wild-type enzyme and mutant enzymes A437G/K540E, A437G, A437G/A581G, S436F/A437G/A613S and S436F/A437G/A613T
sulfachloropyridazine
-
-
Sulfadiazine
-
0.2 mM, complete inhibition
Sulfadiazine
-
0.2 mM, complete inhibition
sulfadimethoxine
-
effective against wild-type enzyme and mutant A437G. Ineffective against mutants A437G/A581G, A437G/K540E, S436F/A437G/A613S and S436F/A437G/A613T
sulfadimethoxine
inhibition of dihydropteroate synthase activity
sulfadoxine
-
-
sulfadoxine
-
effective against wild-type enzyme. Ineffective against mutants A437G, A437G/A581G, A437G/K540E, S436F/A437G/A613S and S436F/A437G/A613T. IC50 for wild-type enzyme: 0.071 mg/ml, IC50 for mutant enzyme A437G: 0.203 mg/ml, IC50 for mutant enzyme A437G/K540E: 0.423 mg/ml, IC50 for mutant enzyme A437G/A581G: 0.775 mg/ml, IC50 for mutant enzymes S436F/A437G/A613S and S436F/A437G/A613T is above 1 mg/ml
sulfadoxine
inhibition of dihydropteroate synthase activity
sulfamerazine
-
effective against wild-type enzyme and mutants A437G/K540E and A437G. Ineffective against mutants A437G/A581G, S436F/A437G/A613S and S436F/A437G/A613T
sulfamethoxazole
-
competitive inhibitor
sulfamethoxazole
-
competitive to 4-aminobenzoate
sulfamethoxazole
-
effective against wild-type enzyme and mutant A437G. Ineffective against mutants A437G/A581G, A437G/K540E, S436F/A437G/A613S and S436F/A437G/A613T
sulfamethoxazole
inhibition of dihydropteroate synthase activity
sulfamethoxazole
a sulfonamide, KD = 2.3 +/-0.1 microM as revealed by fluorescence spectroscopy
sulfamethoxazole
-
competitive inhibitor
sulfamethoxypyridazine
-
sulfamethoxypyridazine
-
-
sulfamoxole
-
-
sulfanilamide
-
-
sulfanilamide
-
effective against wild-type enzyme and mutants A437G/K540E and A437G. Ineffective against mutants A437G/A581G, S436F/A437G/A613S and S436F/A437G/A613T
sulfapyridine
-
-
sulfaquinoxaline
-
effective against wild-type enzyme and mutant A437G. Ineffective against mutants A437G/A581G, A437G/K540E, S436F/A437G/A613S and S436F/A437G/A613T
sulfathiazole
-
competitive inhibitor
sulfathiazole
-
competitive to 4-aminobenzoate
sulfathiazole
-
competitive to 4-aminobenzoate
sulfathiazole
-
competitive to 4-aminobenzoate
sulfathiazole
-
competitive to 4-aminobenzoate
sulfathiazole
-
effective against wild-type enzyme and mutants A437G/K540E and A437G. Ineffective against mutants A437G/A581G, S436F/A437G/A613S and S436F/A437G/A613T
sulfathiazole
inhibition of dihydropteroate synthase activity
sulfathiazole
-
competitive to 4-aminobenzoate
sulfathiazole
-
competitive inhibitor
sulfisomidine
-
competitive inhibitor
sulfisomidine
-
competitive inhibitor
sulfisoxazole
-
effective against wild-type enzyme and mutant A437G. Ineffective against mutants A437G/A581G, A437G/K540E, S436F/A437G/A613S and S436F/A437G/A613T
sulfonamide
-
competitive inhibitor
sulfonamide
-
competitive to 4-aminobenzoate
sulfonamide
-
competitive to 4-aminobenzoate
sulfonamide
-
competitive inhibitor
additional information
no inhibition by sulfadiazine sodium salt, sulfamethoxazole, sulfamethazole, sulfanilamide, sulfathiazole sodium salt in presence of both substrates
-
additional information
-
no inhibition by sulfadiazine sodium salt, sulfamethoxazole, sulfamethazole, sulfanilamide, sulfathiazole sodium salt in presence of both substrates
-
additional information
-
compounds 4-([(2-amino-4-oxo-3,4-dihydro-pyrido[2,3-d]pyrimidin-6-yl)-(2-phosphono-ethyl)-amino]-methyl)-benzoic acid and 4-([(2-amino-4-oxo-3,4-dihydro-pyrido[2,3-d]pyrimidin-6-yl)-(3-phosphono-propyl)-amino]-methyl)-benzoic acid are inactive in inhibition of DHPS, sp2 centers are required at the pterin 5-6 positions for inhibition
-
additional information
-
a series of 4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazines are designed to improve binding affinity as dihydropteroate synthase inhibitors, overview. The N-methyl ring substitution is removed to improve binding within the pterin pocket, and the length of the side chain carboxylic acid is optimized to fully engage the diphosphate binding site. Evaluation by evaluated an enzyme activity assay, X-ray crystallography, isothermal calorimetry, and surface plasmon resonance to obtain a comprehensive understanding of the binding interactions from structural, kinetic, and thermodynamic perspectives
-
additional information
-
structural, computational and mutagenesis studies on the catalytic and resistance mechanisms of DHPS with sulfonamide antibiotics, overview
-
additional information
-
the association rates of pterin diphosphate are mostly unaffected by the osmolytes, except for a 2fold decrease in the presence of 1 M trehalose
-
additional information
computational insights into factor affecting the potency of diaryl sulfone analogs as Escherichia coli dihydropteroate synthase inhibitors. A statistically significant 3D-QSAR model of diaryl sulfone derivatives has been developed. Probable binding and interaction of diaryl sulfone compounds at the catalytic pocket of the enzyme are explored by molecular docking. DFT calculations helped to understand the probable stabilizing factor of the protein-ligand complex which affected the potency of drug candidates. The computed relative free energy difference between most potent and least potent sulfone compounds further emphasized
-
additional information
-
computational insights into factor affecting the potency of diaryl sulfone analogs as Escherichia coli dihydropteroate synthase inhibitors. A statistically significant 3D-QSAR model of diaryl sulfone derivatives has been developed. Probable binding and interaction of diaryl sulfone compounds at the catalytic pocket of the enzyme are explored by molecular docking. DFT calculations helped to understand the probable stabilizing factor of the protein-ligand complex which affected the potency of drug candidates. The computed relative free energy difference between most potent and least potent sulfone compounds further emphasized
-
additional information
-
simultaneously targeting of the two modules of the bifunctional enzyme with pterin binding inhibitors
-
additional information
-
structural, computational and mutagenesis studies on the catalytic and resistance mechanisms of DHPS with sulfonamide antibiotics, overview
-
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0.043
2-amino-4-hydroxy-6-hydroxymethyl-dihydropteridine
-
-
0.0036
6-hydroxymethylpterin monophosphate
100 microM 4-aminobenzoate
0.005 - 0.011
7,8-dihydropteroate
1
p-aminobenzoylglutamate
-
-
0.0082 - 0.023
p-Aminosalicylic acid
0.0015 - 0.94
sulfachloropyridazine
0.0008 - 0.116
sulfadimethoxine
0.0015 - 0.227
sulfadoxine
0.0008 - 0.058
sulfamethazine
0.000028 - 1.17
sulfamethoxazole
0.000025 - 0.0033
sulfamethoxypyridazine
0.0006 - 0.035
sulfamonomethoxine
0.00085 - 0.13
sulfanilamide
0.0016
sulfaquinoxaline
-
-
0.025
sulfaquinoxazoline
-
-
0.00015 - 0.5
sulfathiazole
additional information
additional information
-
0.005 - 0.008
7,8-dihydropteroate
-
inhibitor of p-aminobenzoic acid
0.007 - 0.011
7,8-dihydropteroate
-
inhibitor of 6-hydroxymethyl-7,8-dihydropteridine diphosphate
0.000011
dapsone
-
0.00011
dapsone
-
wild-type enzyme, pH 9.0, 37°C
0.00053
dapsone
-
mutant enzyme V585A, pH 9.0, 37°C
0.00068
dapsone
wild tpye
0.0008
dapsone
wild type enzyme, at pH 9.0 and 37°C
0.0011
dapsone
mutant enzyme K540E, at pH 9.0 and 37°C
0.0014
dapsone
mutant enzyme A613S, at pH 9.0 and 37°C
0.0019
dapsone
mutant enzyme A437G, at pH 9.0 and 37°C
0.00205
dapsone
mutant T557A
0.00367
dapsone
-
mutant enzyme A383G, pH 9.0, 37°C
0.0039
dapsone
mutant enzyme A437G/K540E, at pH 9.0 and 37°C
0.00454
dapsone
-
mutant enzyme A383G/A553G, pH 9.0, 37°C
0.007
dapsone
mutant enzyme A613T, at pH 9.0 and 37°C
0.0148
dapsone
mutant P559S
0.01773
dapsone
-
mutant enzyme S382A/A383G/A553G, pH 9.0, 37°C
0.04
dapsone
mutant enzyme A581G, at pH 9.0 and 37°C
0.058
dapsone
mutant enzyme S436F/A437G/A613S, at pH 9.0 and 37°C
0.156
dapsone
mutant enzyme S436F/A437G/A613T, at pH 9.0 and 37°C
0.177
dapsone
mutant enzyme S436F/A613S, at pH 9.0 and 37°C
0.192
dapsone
mutant enzyme S436F/A613T, at pH 9.0 and 37°C
1.16
dapsone
mutant T557A/P559S
1.29
dapsone
mutant T557V/P559S
0.0082
p-Aminosalicylic acid
-
-
0.023
p-Aminosalicylic acid
-
-
0.0006
Pteroate
mutant enzyme S436F/A437G/A613T, at pH 9.0 and 37°C
0.0009
Pteroate
mutant enzyme S436F/A437G/A613S, at pH 9.0 and 37°C
0.001
Pteroate
mutant enzyme S436A/A437G, at pH 9.0 and 37°C
0.0014
Pteroate
wild type enzyme, at pH 9.0 and 37°C
0.0017
Pteroate
mutant enzyme S436F/A613T, at pH 9.0 and 37°C
0.003
Pteroate
mutant enzyme A613T, at pH 9.0 and 37°C
0.003
Pteroate
mutant enzyme K540E, at pH 9.0 and 37°C
0.0033
Pteroate
mutant enzyme A613S, at pH 9.0 and 37°C
0.0037
Pteroate
mutant enzyme S436F/A613S, at pH 9.0 and 37°C
0.0038
Pteroate
mutant enzyme A437G, at pH 9.0 and 37°C
0.0069
Pteroate
mutant enzyme A437G/K540E, at pH 9.0 and 37°C
0.039
Pteroate
mutant enzyme A581G, at pH 9.0 and 37°C
0.0015
sulfachloropyridazine
-
-
0.00295
sulfachloropyridazine
wild tpye
0.0063
sulfachloropyridazine
mutant T557A
0.0513
sulfachloropyridazine
mutant P559S
0.096
sulfachloropyridazine
mutant T557A/P559S
0.94
sulfachloropyridazine
mutant T557V/P559S
0.0008
sulfadimethoxine
wild type enzyme, at pH 9.0 and 37°C
0.0018
sulfadimethoxine
-
-
0.0024
sulfadimethoxine
mutant enzyme A437G, at pH 9.0 and 37°C
0.014
sulfadimethoxine
mutant enzyme S436A/A437G, at pH 9.0 and 37°C
0.016
sulfadimethoxine
mutant enzyme A437G/K540E, at pH 9.0 and 37°C
0.04
sulfadimethoxine
mutant enzyme S436F/A437G/A613S, at pH 9.0 and 37°C
0.116
sulfadimethoxine
mutant enzyme S436F/A437G/A613T, at pH 9.0 and 37°C
0.0015
sulfadoxine
-
wild-type enzyme, pH 9.0, 37°C
0.003
sulfadoxine
-
mutant enzyme V585A, pH 9.0, 37°C
0.0052
sulfadoxine
mutant enzyme A613T, at pH 9.0 and 37°C
0.007
sulfadoxine
mutant enzyme A437G, at pH 9.0 and 37°C
0.0071
sulfadoxine
wild type enzyme, at pH 9.0 and 37°C
0.0092
sulfadoxine
mutant enzyme A613S, at pH 9.0 and 37°C
0.02
sulfadoxine
mutant enzyme S436A/A437G, at pH 9.0 and 37°C
0.023
sulfadoxine
mutant enzyme K540E, at pH 9.0 and 37°C
0.0481
sulfadoxine
-
mutant enzyme A383G, pH 9.0, 37°C
0.07
sulfadoxine
mutant enzyme A437G/K540E, at pH 9.0 and 37°C
0.084
sulfadoxine
mutant enzyme S436F/A437G/A613S, at pH 9.0 and 37°C
0.086
sulfadoxine
mutant enzyme S436F/A613S, at pH 9.0 and 37°C
0.124
sulfadoxine
mutant enzyme S436F/A613T, at pH 9.0 and 37°C
0.176
sulfadoxine
-
mutant enzyme A383G/A553G, pH 9.0, 37°C
0.196
sulfadoxine
mutant enzyme S436F/A437G/A613T, at pH 9.0 and 37°C
0.198
sulfadoxine
mutant enzyme A581G, at pH 9.0 and 37°C
0.227
sulfadoxine
-
mutant enzyme S382A/A383G/A553G, pH 9.0, 37°C
0.0008
sulfamethazine
wild type enzyme, at pH 9.0 and 37°C
0.0016
sulfamethazine
mutant enzyme A437G, at pH 9.0 and 37°C
0.0071
sulfamethazine
mutant enzyme A437G/K540E, at pH 9.0 and 37°C
0.021
sulfamethazine
mutant enzyme S436F/A437G/A613S, at pH 9.0 and 37°C
0.058
sulfamethazine
mutant enzyme S436F/A437G/A613T, at pH 9.0 and 37°C
0.000028
sulfamethoxazole
-
0.00003
sulfamethoxazole
-
0.00013
sulfamethoxazole
-
-
0.00059
sulfamethoxazole
-
-
0.00371
sulfamethoxazole
mutant T557A
0.0044
sulfamethoxazole
-
-
0.0085
sulfamethoxazole
wild tpye
0.034
sulfamethoxazole
wild type enzyme, at pH 9.0 and 37°C
0.0543
sulfamethoxazole
mutant P559S
0.153
sulfamethoxazole
mutant enzyme A437G, at pH 9.0 and 37°C
0.462
sulfamethoxazole
mutant enzyme S436F/A437G/A613S, at pH 9.0 and 37°C
0.48
sulfamethoxazole
mutant enzyme A437G/K540E, at pH 9.0 and 37°C
0.731
sulfamethoxazole
mutant enzyme S436F/A437G/A613T, at pH 9.0 and 37°C
0.76
sulfamethoxazole
mutant T557V/P559S
1.17
sulfamethoxazole
mutant T557A/P559S
0.000025
sulfamethoxypyridazine
-
0.000031
sulfamethoxypyridazine
-
0.0033
sulfamethoxypyridazine
-
-
0.0006
sulfamonomethoxine
wild type enzyme, at pH 9.0 and 37°C
0.0018
sulfamonomethoxine
mutant enzyme A437G, at pH 9.0 and 37°C
0.0091
sulfamonomethoxine
mutant enzyme A437G/K540E, at pH 9.0 and 37°C
0.014
sulfamonomethoxine
mutant enzyme S436F/A437G/A613S, at pH 9.0 and 37°C
0.035
sulfamonomethoxine
mutant enzyme S436F/A437G/A613T, at pH 9.0 and 37°C
0.00085
sulfanilamide
-
-
0.00015
sulfathiazole
-
wild-type enzyme, pH 9.0, 37°C
0.00019
sulfathiazole
-
mutant enzyme V585A, pH 9.0, 37°C
0.0005
sulfathiazole
wild type enzyme, at pH 9.0 and 37°C
0.0016
sulfathiazole
mutant enzyme A437G, at pH 9.0 and 37°C
0.00295
sulfathiazole
-
mutant enzyme A383G, pH 9.0, 37°C
0.0072
sulfathiazole
mutant enzyme S436A/A437G, at pH 9.0 and 37°C
0.01553
sulfathiazole
-
mutant enzyme A383G/A553G, pH 9.0, 37°C
0.018
sulfathiazole
mutant enzyme A437G/K540E, at pH 9.0 and 37°C
0.019
sulfathiazole
-
mutant enzyme S382A/A383G/A553G, pH 9.0, 37°C
0.025
sulfathiazole
mutant enzyme S436F/A437G/A613T, at pH 9.0 and 37°C
0.027
sulfathiazole
mutant enzyme S436F/A437G/A613S, at pH 9.0 and 37°C
0.5
sulfathiazole
-
resistant enzyme
additional information
additional information
-
KI values of sulfathiazole inhibition on Streptococcus pneumoniae strains with different repeats of amino acids
-
additional information
additional information
-
KI values of sulfathiazole for wild-type and mutant enzyme
-
additional information
additional information
-
KI values of folate derivatives
-
additional information
additional information
-
KI values of sulfadoxine for recombinant enzymes
-
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D96N
-
mutation improves phage display efficiency of the enzyme
D96N/C137I/C172M/C242A
-
130fold improvement in phage display efficiency compared to wild-type enzyme
G58A
site-directed mutagenesis, cannot replace DHPR in Escherichia coli, affects the binding affinity for FMN
K31A
site-directed mutagenesis, can replace DHPR in Escherichia coli, affects the binding affinity for FMN
K51A
site-directed mutagenesis, can replace DHPR in Escherichia coli, affects the binding affinity for FMN
K92E
site-directed mutagenesis, can replace DHPR in Escherichia coli, affects the binding affinity for FMN
M28E
site-directed mutagenesis, can replace DHPR in Escherichia coli, affects the binding affinity for FMN
P55A
mutation associated with dapsone resistance
P55L
mutation associated with dapsone resistance
T53A
mutation associated with dapsone resistance
T53I
mutation associated with dapsone resistance
T53V
mutation associated with dapsone resistance
A437G/A581G
-
mutant enzyme is resistant against inhibition by sulfadoxine, sulfpyridine, sulfadimethoxine, sulfamethoxazole, sulfaquinoxaline and sulfisoxazole (inhibitors of wild-type enzyme)
A581G
the mutation strongly decreases the catalytic efficiency (kcat/Km) of the enzyme with 4-aminobenzoate as substrate
A613T
the mutation slightly decreases the catalytic efficiency (kcat/Km) of the enzyme with 4-aminobenzoate as substrate
DELTA247-306
-
deletion of the parasite-specific insertion: Km values for (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate and p-aminobenzoate are increased compared to mutant DELTA257-306 but still decreased compared to wild type, catalytic efficacy (kcat) is comparable to wild type
DELTA257-306
-
deletion of the parasite-specific insertion: Km values for (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate and p-aminobenzoate are significantly decreased compared to wild type, catalytic efficacy (kcat) is at least 2fold decreased compared to wild type
DELTA74-80
-
deletion of the parasite-specific insertion: Km values for (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate and p-aminobenzoate are 2 to 3 fold higher compared to wild type, catalytic efficacy (kcat) is at least 2fold decreased compared to wild type
DELTA74-86
-
no DHPS activity is detected
K540N
-
parasites collected during October 2005 have mutations associated with a lower level of pyrimethamine resistance and a higher level of sulfadoxine resistance, as well as a novel K540N mutation in PfDHPS gene. The emergence of this parasite population coincides with the widespread use of an additional antifolate drug, trimethoprim-sulfamethoxazole, to treat other infections during January-March 2005
S436A
little association with between mutantion and sulfa drug resistance in patients
S436A/A437G
the mutations increase the catalytic efficiency (kcat/Km) of the enzyme by 1.6fold with 4-aminobenzoate as substrate
S436F/A613S
the mutations strongly decrease the catalytic efficiency (kcat/Km) of the enzyme with 4-aminobenzoate as substrate
S436F/A613T
the mutations strongly decrease the catalytic efficiency (kcat/Km) of the enzyme with 4-aminobenzoate as substrate
A383G/A553G
-
mutation does not much influence the enzyme catalytic activity. Mutant becomes 13fold more resistant to sulfadoxine than the wild type
D459A
high prevalence amino acid mutation observed in Hormozgan Province, southern Iran. The high prevalence of point mutation of Pvdhps genotype necessitates change in programmes and guidelines to eliminate Plasmodium vivax in future
S382A/A383G/A553G
-
mutation does not much influence the enzyme catalytic activity. Mutant becomes 13fold more resistant to sulfadoxine than the wild type
V585A
-
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
-
V585A
-
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
-
P519S
mutant with implicated sulfa drug resistance
P57S
-
the prevalence of DHPS mutations in Pneumocystis jirovecii strains isolated from South African Pneumocystis jirovecii pneumonia patients are examined. Mutations resulting in amino-acid substitutions Thr55Ala and/or Pro57Ser are detected in Pneumocystis jirovecii from 85/151 (56%) patients. The high frequency of PCP episodes with Pneumocystis jirovecii harbouring DHPS mutations in South Africa indicates that populations of this fungus are evolving under considerable selective pressure exerted by sulfa-containing antibiotics
T517A
mutant with implicated sulfa drug resistance
T55A
-
the prevalence of DHPS mutations in Pneumocystis jirovecii strains isolated from South African Pneumocystis jirovecii pneumonia patients are examined. Mutations resulting in amino-acid substitutions Thr55Ala and/or Pro57Ser are detected in Pneumocystis jirovecii from 85/151 (56%) patients. The high frequency of PCP episodes with Pneumocystis jirovecii harbouring DHPS mutations in South Africa indicates that populations of this fungus are evolving under considerable selective pressure exerted by sulfa-containing antibiotics
P559S
mutant with implicated sulfa drug resistance
T557A
mutant with implicated sulfa drug resistance
T557A/P559S
mutant with implicated sulfa drug resistance
T557V/P559S
mutant with implicated sulfa drug resistance
T597V/P599S
-
the mutant has very low p-aminobenzoic acid dependence, short generation time and and high sulfamethoxazole resistance. Upregulated p-aminobenzoic acid synthesis is implicated as a mechanism for sulfa drug resistance
E208K
mutation restores trimethoprim susceptibility closer to wild-type levels while further increasing sulfonamide resistance
F17L
mutation directly lead to sulfonamide resistance while increasing susceptibility to trimethoprim
S18L
mutation directly lead to sulfonamide resistance while increasing susceptibility to trimethoprim
T51M
mutation directly lead to sulfonamide resistance while increasing susceptibility to trimethoprim
GS60
insertion of glycine-serine dipeptide into loop 2 beginning at position 60, sulfonamide resistant, no effect on diphosphate affinity, no effect on 6-hydroxymethyl-7,8-dihydropterin diphosphate binding: KD: 46 +/-5 microM (k(on): 260000 1/M*s, k(off): 12 1/s), reduced binding of p-aminobenzoic acid: KD: 16 +/-6 microM, no detectable binding of sulfamethoxazole
InsY63
insertion of tyrosine residue in loop 2, sulfonamide resistant, no effect on diphosphate affinity, no effect on 6-hydroxymethyl-7,8-dihydropterin diphosphate binding: KD: 48 +/-5 microM (k(on) = 240000 1/M*s, k(off): 11 1/sec), reduced binding of p-aminobenzoic acid: KD: 50 +/-6 microM, no detectable binding of sulfamethoxazole
A437G
-
mutant enzyme is resistant against inhibition by sulfadoxine and sulfpyridine (inhibitors of wild-type enzyme)
A437G
little association with between mutantion and sulfa drug resistance in patients
A437G
mutant enzyme shows increased affinity for 4-aminobenzoate along with reduced binding and efficacy of sulfa drugs. (kcat/Km) for 4-aminobenzoate is increased by 6fold. Mutation enhances the dynamic flexibility of loop D2
A437G/K540E
-
sulfadoxine, sulfpyridine, sulfadimethoxine, sulfamethoxazole, sulfaquinoxaline, sulfisoxazole, sulfanilamide, sulfamerazine, sulfathiazole, dapsone, sulfamoxisole, sulfachloropyridazine and sulfacetamide (inhibitors of wild-type enzyme)
A437G/K540E
the mutations slightly decrease the catalytic efficiency (kcat/Km) of the enzyme with 4-aminobenzoate as substrate
A613S
little association with between mutantion and sulfa drug resistance in patients
A613S
the mutation strongly decreases the catalytic efficiency (kcat/Km) of the enzyme with 4-aminobenzoate as substrate
K540E
-
correlation of polymorphisms in Plasmodium falciparum dihydropteroate synthase and in vitro parasite susceptibility to sulfadoxine and pyrimethamine and in vivo treatment are analyzed: Patients with the dihydropteroate synthase K540E mutation are 2.6times as likely to fail treatment compared to patients having wild-type form form
K540E
the mutation strongly decreases the catalytic efficiency (kcat/Km) of the enzyme with 4-aminobenzoate as substrate
S436F/A437G/A613S
-
sulfadoxine, sulfpyridine, sulfadimethoxine, sulfamethoxazole, sulfaquinoxaline, sulfisoxazole, sulfanilamide, sulfamerazine, sulfathiazole and dapsone (inhibitors of wild-type enzyme)
S436F/A437G/A613S
the mutations increase the catalytic efficiency (kcat/Km) of the enzyme by 2fold with 4-aminobenzoate as substrate
S436F/A437G/A613T
-
sulfadoxine, sulfpyridine, sulfadimethoxine, sulfamethoxazole, sulfaquinoxaline, sulfisoxazole, sulfanilamide, sulfamerazine, sulfathiazole and dapsone (inhibitors of wild-type enzyme)
S436F/A437G/A613T
the triple mutant exhibits lower Km value for 4-aminobenzoate than the wild type enzyme. The mutations slightly increase the catalytic efficiency (kcat/Km) of the enzyme
A383G
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
A383G
high prevalence amino acid mutation observed in Hormozgan Province, southern Iran. The high prevalence of point mutation of Pvdhps genotype necessitates change in programmes and guidelines to eliminate Plasmodium vivax in future
A383G
-
mutation does not much influence the enzyme catalytic activity. Mutant becomes 13fold more resistant to sulfadoxine than the wild type
A383G
the mutation confers resistance to sulfadoxine
A383G
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
A553G
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
A553G
the mutation confers resistance to sulfadoxine
A553G
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
K512D
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
K512D
the mutation confers resistance to sulfadoxine
K512D
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
K512E
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
K512E
the mutation confers resistance to sulfadoxine
K512E
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
S382A
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
S382A
the mutation confers resistance to sulfadoxine
S382A
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
V585A
-
2fold increase in the level of resistance to sulfadoxine compared with that of the wild type carrying V585A. V585A mutant is 4fold more resistant to dapsone than the wild type
V585A
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
V585A
the mutation confers resistance to sulfadoxine
V585A
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
A383G
-
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
-
A383G
-
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
-
S382A
-
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
-
S382A
-
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
-
A383G
-
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
-
A383G
-
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
-
S382A
-
drug resistance mutation. Resistance mutations subtly alters the intricate enzyme/4-aminobenzoate/sulfadoxine interactions such that DHPS affinity for 4-aminobenzoate is diminished only moderately, but its affinity for sulfadoxine is changed substantially
-
S382A
-
dominant drug resistance mutation. Mutation subtly alters the intricate enzyme-4-amino benzoic acid-sulfadoxine interactions such that DHPS affinity for 4-amino benzoic acid is diminished only moderately, but its affinity for sulfadoxine is changed substantially
-
additional information
bifunctional enzyme, mitochondrial enzyme ubiquitously expressed, cytosolic enzyme only in reproductive tisse, construction of a chimeric protein containing the first 224 amino acids of cytosolic DHPS fused to GFP, expression in Arabidopsis thaliana, Arabidopsis thaliana mutant lacking DHPS indicates a role of DHPS in seed stress
additional information
-
difference analysis in gene expression in Haemophilus parasuis serovar 1, 2, 3 and 5
additional information
DHPS contains also dihydropteroate reductase activity
additional information
-
DHPS contains also dihydropteroate reductase activity
additional information
detection of mutations to predict dapsone resistance
additional information
-
detection of mutations to predict dapsone resistance
additional information
assessment of mutations in DHPS in West Africa
additional information
-
assessment of mutations in DHPS in West Africa
additional information
assessment of mutations in DHPS associated with antifolate resistance in several geographical regions
additional information
-
assessment of mutations in DHPS associated with antifolate resistance in several geographical regions
additional information
coupled enzymatic spectrophotometric assay to measure the activity of DHPS
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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
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
Volpe, F.; Ballantine, S.P.; Delves, C.J.
The multifunctional folic acid synthesis fas gene of Pneumocystis carinii encodes dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase
Eur. J. Biochem.
216
449-458
1993
Pneumocystis carinii
brenda
Richey, D.P.; Brown, G.M.
The biosynthesis of folic acid. IX. Purification and properties of the enzymes required for the formation of dihydropteroic acid
J. Biol. Chem.
244
1582-1592
1969
Escherichia coli
brenda
Richey, D.P.; Brown, G.M.
Hydroxymethyldihydropteridine pyrophosphokinase and dihydropteroate synthetase from Escherichia coli
Methods Enzymol.
18B
765-771
1971
Escherichia coli
-
brenda
McCullough, J.L.; Maren, T.H.
Dihydropteroate synthetase from Plasmodium berghei: isolation, properties, and inhibition by dapsone and sulfadiazine
Mol. Pharmacol.
10
140-145
1974
Plasmodium berghei
brenda
Walter, R.D.; Knigk, E.
Biosynthesis of folic acid compounds in plasmodia. Purification and properties of the 7,8-dihydropteroate-synthesizing enzyme from Plasmodium chabaudi
Hoppe-Seyler's Z. Physiol. Chem.
355
431-437
1974
Plasmodium chabaudi
brenda
Walter, R.D.; Knigk, E.
7,8-Dihydropteroate-synthesizing enzyme from Plasmodium chabaudi
Methods Enzymol.
66
564-570
1980
Plasmodium chabaudi
brenda
Talarico, T.L.; Dev, I.K.; Dallas, W.S.; Ferone, R.; Ray, P.H.
Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100
J. Bacteriol.
173
7029-7032
1991
Escherichia coli MC4100 (P0AC13), Escherichia coli MC4100
brenda
Triglia, T.; Menting, J.G.T.; Wilson, C.; Cowman, A.F.
Mutations in dihydropteroate synthase are responsible for sulfone and sulfonamide resistance in Plasmodium falciparum
Proc. Natl. Acad. Sci. USA
94
13944-13949
1997
Plasmodium falciparum
brenda
Rebeille, F.; Macherel, D.; Mouillon, J.M.; Garin, J.; Douce, R.
Folate biosynthesis in higher plants: purification and molecular cloning of a bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase localized in mitochondria
EMBO J.
16
947-957
1997
Pisum sativum
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Bacillus anthracis (Q81VW8), Bacillus anthracis
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Bacillus anthracis
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Bacillus anthracis, Yersinia pestis
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Bacillus anthracis, Yersinia pestis
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Yersinia pestis (A0A384KP04), Yersinia pestis, Bacillus anthracis (Q81VW8)
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Escherichia coli (P0AC13), Escherichia coli, Escherichia coli K12 (P0AC13)
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Staphylococcus aureus (O05701), Staphylococcus aureus
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Plasmodium vivax, Plasmodium vivax (A5JZS1), Plasmodium vivax Salvador I (A5JZS1)
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Helicobacter pylori (G2MFH6), Helicobacter pylori, Helicobacter pylori SNT49 (G2MFH6), Yersinia pestis (A0A384KP04)
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Plasmodium vivax (Q6Y3G8), Plasmodium vivax
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Yersinia pestis (A0A384KP04)
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