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.
2 biopterin + 3 NADPH + 3 H+
dihydrobiopterin + tetrahydrobiopterin + 3 NADP+
6-biopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
7,8-dihydroneopterin + NADPH + H+
5,6,7,8-tetrahydroneopterin + NADP+
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
biopterin + NADPH + H+
7,8-dihydrobiopterin + NADP+
biopterin + NADPH + H+
dihydrobiopterin + NADP+
dihydrobiopterin + NADPH
5,6,7,8-tetrahydrobiopterin + NADP+
Dihydrobiopterin + NADPH
?
dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
Dihydrofolate + NADPH
5,6,7,8-Tetrahydrofolate + NADP+
Dihydroneopterin + NADPH
?
dihydrosepiapterin + NADPH
?
folate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
folate + NADPH + H+
7,8-dihydrofolate + NADP+
folate + NADPH + H+
7,8-dihydrofolate + tetrahydrofolate + NADP+
quinonoid 6,7-dimethyl-7,8-dihydropterin + NADPH + H+
?
quinonoid dihydrobiopterin + NADPH + H+
tetrahydrobiopterin + NADP+
additional information
?
-
2 biopterin + 3 NADPH + 3 H+
dihydrobiopterin + tetrahydrobiopterin + 3 NADP+
essential enzyme of pterin and folate metabolism
-
-
?
2 biopterin + 3 NADPH + 3 H+
dihydrobiopterin + tetrahydrobiopterin + 3 NADP+
-
salvage of pterins, enzyme acts as a metabolic bypass for drugs targeting dihydrofolate reductase, PTR1 contributes about 10% of the reduction of folates in wild-type cells while the remaining 90% is due to the activity of dihydrofolate reductase-thymidylate synthase (EC 1.5.1.3)
-
-
?
6-biopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
6-biopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
low activity
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
low activity
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
cf. EC 1.5.1.50, moderate activity
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
cf. EC 1.5.1.50, moderate activity
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
cf. EC 1.5.1.50, moderate activity
-
-
?
7,8-dihydroneopterin + NADPH + H+
5,6,7,8-tetrahydroneopterin + NADP+
stereoisomer of biopterin, moderate activity
-
-
?
7,8-dihydroneopterin + NADPH + H+
5,6,7,8-tetrahydroneopterin + NADP+
stereoisomer of biopterin, moderate activity
-
-
?
7,8-dihydroneopterin + NADPH + H+
5,6,7,8-tetrahydroneopterin + NADP+
stereoisomer of biopterin, moderate activity
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
substrate binding structure
-
-
?
Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
-
-
-
?
Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
-
-
-
-
?
Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
-
activity with NADH is less than 5% of the activity with NADPH
-
-
?
Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
-
-
-
-
?
Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
2-step reaction via intermediate 7,8-dihydrobiopterin
-
-
?
Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
-
-
-
-
?
Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
-
no activity with NADH and NADP+
-
-
?
Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
-
no activity with NADH and NADP+
-
-
?
biopterin + NADPH + H+
7,8-dihydrobiopterin + NADP+
-
-
-
?
biopterin + NADPH + H+
7,8-dihydrobiopterin + NADP+
best substrate
-
-
?
biopterin + NADPH + H+
7,8-dihydrobiopterin + NADP+
-
-
-
?
biopterin + NADPH + H+
dihydrobiopterin + NADP+
-
-
-
-
?
biopterin + NADPH + H+
dihydrobiopterin + NADP+
-
-
-
?
biopterin + NADPH + H+
dihydrobiopterin + NADP+
-
-
-
-
?
biopterin + NADPH + H+
dihydrobiopterin + NADP+
-
-
-
?
dihydrobiopterin + NADPH
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
-
?
dihydrobiopterin + NADPH
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
r
Dihydrobiopterin + NADPH
?
-
-
-
-
?
Dihydrobiopterin + NADPH
?
-
-
-
-
?
Dihydrobiopterin + NADPH
?
-
-
-
-
?
Dihydrobiopterin + NADPH
?
-
-
-
-
?
dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
-
?
dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
-
?
dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
Dihydrofolate + NADPH
5,6,7,8-Tetrahydrofolate + NADP+
-
-
-
-
?
Dihydrofolate + NADPH
5,6,7,8-Tetrahydrofolate + NADP+
-
-
-
?
Dihydrofolate + NADPH
5,6,7,8-Tetrahydrofolate + NADP+
-
-
-
-
?
Dihydrofolate + NADPH
5,6,7,8-Tetrahydrofolate + NADP+
-
-
-
-
?
Dihydrofolate + NADPH
5,6,7,8-Tetrahydrofolate + NADP+
-
-
-
-
?
Dihydroneopterin + NADPH
?
-
-
-
-
?
Dihydroneopterin + NADPH
?
-
-
-
-
?
Dihydroneopterin + NADPH
?
-
no activity
-
-
?
dihydrosepiapterin + NADPH
?
-
-
-
-
?
dihydrosepiapterin + NADPH
?
-
-
-
-
?
dihydrosepiapterin + NADPH
?
-
no activity
-
-
?
folate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
?
folate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
-
?
folate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
?
folate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
?
folate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
-
?
folate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
-
?
folate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
-
?
folate + NADPH
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
-
?
folate + NADPH + H+
7,8-dihydrofolate + NADP+
high activity, see also EC 1.5.1.3
-
-
?
folate + NADPH + H+
7,8-dihydrofolate + NADP+
reaction of EC 1.5.1.3
-
-
?
folate + NADPH + H+
7,8-dihydrofolate + NADP+
-
-
-
?
folate + NADPH + H+
7,8-dihydrofolate + tetrahydrofolate + NADP+
-
-
-
-
?
folate + NADPH + H+
7,8-dihydrofolate + tetrahydrofolate + NADP+
essential enzyme of pterin and folate metabolism
-
-
?
quinonoid 6,7-dimethyl-7,8-dihydropterin + NADPH + H+
?
-
-
-
-
?
quinonoid 6,7-dimethyl-7,8-dihydropterin + NADPH + H+
?
-
-
-
-
?
quinonoid dihydrobiopterin + NADPH + H+
tetrahydrobiopterin + NADP+
-
-
-
-
?
quinonoid dihydrobiopterin + NADPH + H+
tetrahydrobiopterin + NADP+
-
-
-
-
?
additional information
?
-
enzyme PruA does not exhibit pteridine reductase activity with 7,8-dihydrofolate or fully oxidized pterins. PruA exhibits maximal catalytic efficiency with H2BPt, while both H2MPt and 7,8-dihydroneopterin (H2NPt) also serve as competent substrates. Substrate specificity, overview. No activity with 7,8-dihydrofolate, biopterin, and folate
-
-
-
additional information
?
-
enzyme PruA does not exhibit pteridine reductase activity with 7,8-dihydrofolate or fully oxidized pterins. PruA exhibits maximal catalytic efficiency with H2BPt, while both H2MPt and 7,8-dihydroneopterin (H2NPt) also serve as competent substrates. Substrate specificity, overview. No activity with 7,8-dihydrofolate, biopterin, and folate
-
-
-
additional information
?
-
enzyme PruA does not exhibit pteridine reductase activity with 7,8-dihydrofolate or fully oxidized pterins. PruA exhibits maximal catalytic efficiency with H2BPt, while both H2MPt and 7,8-dihydroneopterin (H2NPt) also serve as competent substrates. Substrate specificity, overview. No activity with 7,8-dihydrofolate, biopterin, and folate
-
-
-
additional information
?
-
enzyme is associated with folate metabolism, responsible for salvage of pterins and reduction of folates
-
-
?
additional information
?
-
-
enzyme is associated with folate metabolism, responsible for salvage of pterins and reduction of folates
-
-
?
additional information
?
-
NADPH binds first, the enzyme-NADPH complex binds the substrate
-
-
?
additional information
?
-
-
NADPH binds first, the enzyme-NADPH complex binds the substrate
-
-
?
additional information
?
-
substrate specificity, overview
-
-
-
additional information
?
-
-
no activity with quinoid dihydrobiopterin
-
-
?
additional information
?
-
-
primary enzyme mediating pteridine salvage
-
-
?
additional information
?
-
-
the enzyme mediates the synthesis of tetrahydropteridines
-
-
?
additional information
?
-
essential for the salvage of pterins
-
-
?
additional information
?
-
-
essential for the salvage of pterins
-
-
?
additional information
?
-
-
thermal shift enzyme assay optimization
-
-
?
additional information
?
-
enzyme PTR1 synthesizes the formation of tetrahydrobiopterin from biopterin via dihydrobiopterin or from the quinoide form dihydrobiopterin, pathway overview
-
-
-
additional information
?
-
-
enzyme PTR1 synthesizes the formation of tetrahydrobiopterin from biopterin via dihydrobiopterin or from the quinoide form dihydrobiopterin, pathway overview
-
-
-
additional information
?
-
7,8-dihydro-L-biopterin and pyrimethamine (PMA) interact with enzyme residues S112, Y194, L226, and S227, molecular dynamics and docking study, overview
-
-
-
additional information
?
-
-
7,8-dihydro-L-biopterin and pyrimethamine (PMA) interact with enzyme residues S112, Y194, L226, and S227, molecular dynamics and docking study, overview
-
-
-
additional information
?
-
-
the enzyme mediates the synthesis of tetrahydropteridines
-
-
?
additional information
?
-
enzyme is used by the organism to bypass antifolate inhibition, catalytic pathway
-
-
?
additional information
?
-
-
enzyme is used by the organism to bypass antifolate inhibition, catalytic pathway
-
-
?
additional information
?
-
enzyme PTR1 synthesizes the formation of tetrahydrobiopterin from biopterin via dihydrobiopterin or from the quinoide form dihydrobiopterin, pathway overview
-
-
-
additional information
?
-
-
the enzyme is involved in the resistance to the methotrexate, aminopterin and trimethoprim antifolates
-
-
?
additional information
?
-
-
essential for the salvage of pterins
-
-
?
additional information
?
-
-
the enzyme is involved in the resistance to the methotrexate, aminopterin and trimethoprim antifolates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 biopterin + 3 NADPH + 3 H+
dihydrobiopterin + tetrahydrobiopterin + 3 NADP+
6-biopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
biopterin + NADPH + H+
7,8-dihydrobiopterin + NADP+
biopterin + NADPH + H+
dihydrobiopterin + NADP+
dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
folate + NADPH + H+
7,8-dihydrofolate + NADP+
folate + NADPH + H+
7,8-dihydrofolate + tetrahydrofolate + NADP+
additional information
?
-
2 biopterin + 3 NADPH + 3 H+
dihydrobiopterin + tetrahydrobiopterin + 3 NADP+
essential enzyme of pterin and folate metabolism
-
-
?
2 biopterin + 3 NADPH + 3 H+
dihydrobiopterin + tetrahydrobiopterin + 3 NADP+
-
salvage of pterins, enzyme acts as a metabolic bypass for drugs targeting dihydrofolate reductase, PTR1 contributes about 10% of the reduction of folates in wild-type cells while the remaining 90% is due to the activity of dihydrofolate reductase-thymidylate synthase (EC 1.5.1.3)
-
-
?
6-biopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
6-biopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
-
?
biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
-
-
-
?
biopterin + NADPH + H+
7,8-dihydrobiopterin + NADP+
-
-
-
?
biopterin + NADPH + H+
7,8-dihydrobiopterin + NADP+
-
-
-
?
biopterin + NADPH + H+
dihydrobiopterin + NADP+
-
-
-
?
biopterin + NADPH + H+
dihydrobiopterin + NADP+
-
-
-
?
dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
-
-
-
?
folate + NADPH + H+
7,8-dihydrofolate + NADP+
reaction of EC 1.5.1.3
-
-
?
folate + NADPH + H+
7,8-dihydrofolate + NADP+
-
-
-
?
folate + NADPH + H+
7,8-dihydrofolate + tetrahydrofolate + NADP+
-
-
-
-
?
folate + NADPH + H+
7,8-dihydrofolate + tetrahydrofolate + NADP+
essential enzyme of pterin and folate metabolism
-
-
?
additional information
?
-
enzyme is associated with folate metabolism, responsible for salvage of pterins and reduction of folates
-
-
?
additional information
?
-
-
enzyme is associated with folate metabolism, responsible for salvage of pterins and reduction of folates
-
-
?
additional information
?
-
-
primary enzyme mediating pteridine salvage
-
-
?
additional information
?
-
-
the enzyme mediates the synthesis of tetrahydropteridines
-
-
?
additional information
?
-
essential for the salvage of pterins
-
-
?
additional information
?
-
-
essential for the salvage of pterins
-
-
?
additional information
?
-
enzyme PTR1 synthesizes the formation of tetrahydrobiopterin from biopterin via dihydrobiopterin or from the quinoide form dihydrobiopterin, pathway overview
-
-
-
additional information
?
-
-
enzyme PTR1 synthesizes the formation of tetrahydrobiopterin from biopterin via dihydrobiopterin or from the quinoide form dihydrobiopterin, pathway overview
-
-
-
additional information
?
-
-
the enzyme mediates the synthesis of tetrahydropteridines
-
-
?
additional information
?
-
enzyme is used by the organism to bypass antifolate inhibition, catalytic pathway
-
-
?
additional information
?
-
-
enzyme is used by the organism to bypass antifolate inhibition, catalytic pathway
-
-
?
additional information
?
-
enzyme PTR1 synthesizes the formation of tetrahydrobiopterin from biopterin via dihydrobiopterin or from the quinoide form dihydrobiopterin, pathway overview
-
-
-
additional information
?
-
-
the enzyme is involved in the resistance to the methotrexate, aminopterin and trimethoprim antifolates
-
-
?
additional information
?
-
-
essential for the salvage of pterins
-
-
?
additional information
?
-
-
the enzyme is involved in the resistance to the methotrexate, aminopterin and trimethoprim antifolates
-
-
?
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.
(-)-epicatechin-3-gallate
-
(1R,4S,6R)-4-hydroxy-3-methyl-6-(propan-2-yl)cyclohex-2-en-1-yl 5beta,8alpha,10alpha,13alpha-kaura-9(11),16-dien-18-oate
-
(1R,4S,6R)-4-hydroxy-3-methyl-6-(propan-2-yl)cyclohex-2-en-1-yl 5beta,8alpha,9beta,10alpha,13alpha-kaur-16-en-18-oate
-
(2-amino-2,3-dihydro-1H-benzimidazol-1-yl)(phenyl)methanone
-
-
(2E,4E)-N-(2-methylpropyl)dodeca-2,4-dienamide
-
-
(2E,4E)-N-(2-methylpropyl)octadeca-2,4-dienamide
-
-
(2E,4E,12E)-13-(benzo[d][1,3]dioxol-5-yl)-N-isobutyltrideca-2,4,12-trienamide
-
-
(4-fluoro-phenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydro-pyrimidine-5-carboxylic acid ethyl ester
-
-
(4-fluoro-phenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylic acid ethyl ester
-
treatment with 98 microM resulted in reduction of viable cells from 96.5% (control) to 9.86% after 5 h
(4S)-4-[[(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]phenyl)carbonyl]amino]-5-oxohexanoic acid
(Z)-5-(2,4-dichlorobenzylidene)-thiazolidine-2,4-dione
-
-
(Z)-5-(2-bromo-5-methoxybenzylidene)-thiazolidine-2,4-dione
-
-
(Z)-5-(2-bromo-6-fluorobenzylidene)-thiazolidine-2,4-dione
-
-
(Z)-5-(2-hydroxy-3-bromo-5-chlorobenzylidene)-thiazolidine-2,4-dione
-
a noncompetitive inhibitor that binds in the same site as the cofactor
(Z)-5-(2-hydroxy-5-chlorobenzylidene)-thiazolidine-2,4-dione
-
-
([5-[(1H-benzimidazol-2-yl)methyl]-1,3,4-oxadiazol-2-yl]sulfanyl)acetic acid
-
-
([5-[(1H-benzimidazol-2-yl)methyl]-4H-1,2,4-triazol-3-yl]sulfanyl)acetic acid
-
-
([5-[(6-nitro-1H-benzimidazol-2-yl)methyl]-1,3,4-oxadiazol-2-yl]sulfanyl)acetic acid
-
-
([5-[(6-nitro-1H-benzimidazol-2-yl)methyl]-4H-1,2,4-triazol-3-yl]sulfanyl)acetic acid
-
-
1-(2,5-dichlorobenzyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
-
1-(2-chlorobenzyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
-
1-(2-fluorobenzyl)-1H-benzimidazol-2-amine
-
-
1-(2-methylbenzyl)-1H-benzimidazol-2-amine
-
-
1-(2-phenylethyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
-
1-(3,4-dichlorobenzyl)-1H-benzimidazol-2-amine
-
-
1-(3,4-dichlorobenzyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
-
1-(3,4-dichlorobenzyl)-4-methoxy-1H-benzimidazol-2-amine
-
-
1-(3,4-dichlorobenzyl)-4-phenyl-1H-benzimidazol-2-amine
-
-
1-(3,4-dichlorobenzyl)-4-propoxy-1H-benzimidazol-2-amine
-
-
1-(3,4-dichlorobenzyl)-5,6-dimethyl-1H-benzimidazol-2-amine
-
-
1-(3,4-dichlorobenzyl)-7-methoxy-1H-benzimidazol-2-amine
-
-
1-(3,4-dichlorobenzyl)-7-phenyl-1H-benzimidazol-2-amine
-
-
1-(3,4-dichlorobenzyl)-7-propoxy-1H-benzimidazol-2-amine
-
-
1-(3,4-dichlorophenyl)-6,6-dimethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine
competitive inhibition
1-(3,4-dichlorophenyl)-6-(4-nitrophenyl)-1,6-dihydro-1,3,5-triazine-2,4-diamine
competitive inhibition
-
1-(3,4-methylenedioxyphenyl)-(1E)-tetradecene
-
-
1-(3,5-dichlorobenzyl)-1H-benzimidazol-2-amine
-
-
1-(3-chlorobenzyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
-
1-(4-bromobenzyl)-1H-benzimidazol-2-amine
-
-
1-(4-chlorobenzyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
-
1-(4-chlorophenyl)-6-methyl-1,6-dihydro-1,3,5-triazine-2,4-diamine
competitive inhibition
-
1-(4-chlorophenyl)-6-propyl-1,6-dihydro-1,3,5-triazine-2,4-diamine
competitive inhibition
-
1-(4-methoxyphenyl)-6,6-dimethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine
competitive inhibition
-
1-(4-methylbenzyl)-1H-benzimidazol-2-amine
-
-
1-(4-tert-butylbenzyl)-1H-benzimidazol-2-amine
-
-
1-(naphthalen-1-ylmethyl)-1H-benzimidazol-2-amine
-
-
1-(naphthalen-2-ylmethyl)-1H-benzimidazol-2-amine
-
-
1-(pyridin-2-yl)-1H-benzimidazol-2-amine
-
-
1-(pyridin-3-yl)-1H-benzimidazol-2-amine
-
-
1-benzyl-2,3-dihydro-1H-benzimidazol-2-amine
-
-
1-ethyl-2,3-dihydro-1H-benzimidazol-2-amine
-
-
1-[(4-[[6-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-4-carboxylic acid
1-[(4-[[8-amino-3-phenyl-6-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-4-carboxylic acid
1-[3-(trifluoromethyl)benzyl]-1H-benzimidazol-2-amine
-
-
1H-benzimidazol-2-amine
-
-
2,4,6-triaminoquinazoline
i.e. TAQ, mimics the pterin head group of methotrexate, binds to the active site, binding structure and inhibition mechanism
2,4-diamino-6-bromo-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2,4-diamino-6-[(E)-2-phenylethenyl]-7H-pyrrolo[2,3-d]-pyrimidine-5-carbonitrile
-
-
2,4-diamino-6-[(Z)-2-(4-methylphenyl)ethenyl]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2,4-diamino-6-[(Z)-2-phenylethenyl]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2,4-diamino-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2,4-Diaminopteridines
-
overview
2,4-diaminopyrimido[4,5-b]indol-6-ol
synthesis, inhibits TbPTR1 activity by competitive inhibition, binding mode, and structural characterization of its ternary complex with TbPTR1 and the cofactor NADP(H) from crystal structure, overview. The compound adopts a substrate-like orientation inside the cavity that maximizes the binding contributions of hydrophobic and hydrogen-bond interactions
-
2,4-Diaminoquinazolines
-
overview
2,6-dimethyl [3-O-benzyl-1,2-O isopropylidene-beta-L-threo-pentofuronose-4-yl]-1-phenyl-1,4-dihydro pyridine-3,5-dicarboxylic acid diethyl ether
-
-
2,6-dimethyl-4-(3-O-benzyl-1,2-O-isopropylidene-beta-L-threo pentofuranos-4-yl)-1-phenyl-1,4-dihydro-pyridine-3,5-dicarboxylic acid diethyl ester
-
oral therapy shows apoptosis like phenotypes targeting pteridine reductase 1 in intracellular amastigotes
2,6-dimethyl-4-(3-O-benzyl-1,2-ortho-isopropylidene-beta-L-threopentofuranos-4-yl)-1-phenyl-1,4-dihydro-pyridine-3,5-dicarboxylic acid diethyl ester
treatment with 90 microM GDA resulted in reduction of viable cells from 94.2% (control) to 77.1%, 76.8%, 74.9%, 35.3% and 24.9% at 18, 24, 48, 72 and 96 h, respectively
2-(3,4-dihydroxyphenyl)-3,6-dihydroxy-4H-1-benzopyran-4-one
2-(3,4-dihydroxyphenyl)-6-hydroxy-2,3-dihydro-4H-1-benzopyran-4-one
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidine-4-thione
2-amino-4-(1-pyrrolidinyl)-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-4-(cyclopentyloxy)-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-4-(thiomorpholin-4-yl)-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-4-methoxy-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
2-amino-4-oxo-6-phenyl-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
2-amino-4-oxo-6-[(E)-2-phenylethenyl]-4,7-dihydro-3Hpyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-4-[(propan-2-yl)oxy]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-5,6-bis(4-chlorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-5,6-bis(4-fluorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-5,6-bis(4-methylphenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-5,6-diphenyl-3,7-dihydro-4H-pyrrolo[2,3-d]-pyrimidin-4-one
-
-
2-amino-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
2-amino-5-(3-chlorophenyl)-6-(4-fluorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-5-(4-fluorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-5-(4-methylphenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-5-methyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-5-methyl-6-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-6-(1,3-benzodioxol-5-yl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
2-amino-6-(3-formylphenyl)-4-(1-pyrrolidinyl)-7H-pyrrolo-[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-6-(3-formylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
2-amino-6-(4-bromophenyl)-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-6-(4-ethylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
2-amino-6-(4-fluorophenyl)-5-(4-methoxyphenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-6-(4-fluorophenyl)-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-6-(4-methoxyphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
2-amino-6-bromo-4-(1-pyrrolidinyl)-7H-pyrrolo[2,3-d]-pyrimidine-5-carbonitrile
-
-
2-amino-6-bromo-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
2-amino-6-phenyl-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-6-[3-(methanesulfonyl)phenyl]-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-6-[4-(2-methylpropyl)phenyl]-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-6-[4-(methanesulfonyl)phenyl]-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-6-[4-[3-(4-morpholinyl)propyl]phenyl]-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one trifluoroacetate
-
-
22-phenyl[11,21:24,31-terphenyl]-13,15,34-triol
-
3,6-dihydroxy-2-(3-hydroxyphenyl)-4H-1-benzopyran-4-one
3alpha-cinnamoyloxy-9beta-hydroxy-ent-kaur-16-en-19-oic acid
-
3alpha-cinnamoyloxy-ent-kaur-16-en-19-oic acid
-
3alpha-p-coumaroyloxy-9beta-hydroxy-entkaur-16-en-19-oic acid
-
3alpha-p-coumaroyloxy-ent-kaur-16-en-19-oic acid
-
4-(1-pyrrolidinyl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine
-
-
4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydro-4H-pyrimidin-5-carboxylic acid ethyl ester
-
both monastrol (R) and (S) enantiomers fit well in the ligand-binding pocket of LdPTR1. Monastrol is a potent inhibitor of PTR1 in Leishmania, it inhibits proliferation of amastigotes in macrophage cultures infected with an Leishmania donovani clinical isolate, with no host cytotoxicity
4-(4,6-diamino-2,2-dimethyl-1,3,5-triazin-1(2H)-yl)phenol
competitive inhibition
-
4-(benzyloxy)-1-(3,4-dichlorobenzyl)-1H-benzimidazol-2-amine
-
-
4-(benzyloxy)pyrimidine-2,6-diamine
-
4-(thiomorpholin-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine
-
-
4-chloro-1-(3,4-dichlorobenzyl)-1H-benzimidazol-2-amine
-
-
5,6-bis(4-chlorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5,6-bis(4-chlorophenyl)-N~4~,N~4~-dimethyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5,6-bis(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5,6-bis(4-fluorophenyl)-N~4~,N~4~-dimethyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5,6-bis(4-methylphenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5-(3,4-dichlorobenzylidene)-thiazolidine-2,4-dione
-
-
5-(3-chlorophenyl)-6-(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5-(4-chlorophenyl)-1,3,5-triazaspiro[5.5]undeca-1,3-diene-2,4-diamine
competitive inhibition
-
5-(4-fluorophenyl)-4-(2-methylpropoxy)-7H-pyrrolo[2,3-d]pyrimidin-2-amine
-
-
5-(4-fluorophenyl)-4-isopropyloxy-7H-pyrrolo[2,3-d]-pyrimidin-2-amine
-
-
5-(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5-(4-methylphenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5-(phenylethynyl)-4-(1-pyrrolidinyl)-7H-pyrrolo[2,3-d]-pyrimidin-2-amine
-
-
5-Deaza-5,6,7,8-tetrahydrofolate
-
-
5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
5-[(1H-benzimidazol-2-yl)methyl]-1,3,4-oxadiazol-2-amine
-
-
5-[(1H-benzimidazol-2-yl)methyl]-1,3,4-oxadiazole-2-thiol
-
-
5-[(1H-benzimidazol-2-yl)methyl]-4H-1,2,4-triazol-3-amine
-
-
5-[(1H-benzimidazol-2-yl)methyl]-4H-1,2,4-triazole-3-thiol
-
-
5-[(6-chloro-1H-benzimidazol-2-yl)methyl]-1,3,4-oxadiazole-2-thiol
-
-
5-[(6-chloro-1H-benzimidazol-2-yl)methyl]-4H-1,2,4-triazole-3-thiol
-
-
5-[(6-nitro-1H-benzimidazol-2-yl)methyl]-1,3,4-oxadiazol-2-amine
-
-
5-[(6-nitro-1H-benzimidazol-2-yl)methyl]-1,3,4-oxadiazole-2-thiol
-
-
5-[(6-nitro-1H-benzimidazol-2-yl)methyl]-4H-1,2,4-triazol-3-amine
-
-
5-[(6-nitro-1H-benzimidazol-2-yl)methyl]-4H-1,2,4-triazole-3-thiol
-
-
6,6'-[1,4-phenylenebis(methyleneazanediyl)]bis(N-benzylhexanamide)
-
6,6'-[methylenebis[(4,1-phenylene)methyleneazanediyl]]bis(N-benzylhexanamide)
-
6,6'-[[1,1'-biphenyl]-4,4'-diylbis(methyleneazanediyl)]bis(N-benzylhexanamide)
-
6,7-di(propan-2-yl)pteridine-2,4-diamine
6-(4-bromophenyl)-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
6-(4-fluorophenyl)-5-(4-methoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
6-(4-fluorophenyl)-5-(4-methoxyphenyl)-N4,N4-dimethyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
6-(4-fluorophenyl)-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
6-(4-fluorophenyl)-N~4~,N~4~-dimethyl-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
6-(benzylsulfanyl)pyrimidine-2,4-diamine
6-hydroxy-2-(3-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
6-hydroxy-2-(4-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
6-methyl-7-(propan-2-yl)pteridine-2,4-diamine
6-phenylpteridine-2,4,7-triamine
6-[(3aR,9bS)-2,3,3a,9b-tetrahydro[1]benzopyrano[4,3-b]pyrrol-1(4H)-yl]hexan-1-amine
-
6-[(4-methoxybenzyl)sulfanyl]pyrimidine-2,4-diamine
6-[(4-methoxyphenyl)methoxy]pyrimidine-2,4-diamine
-
6-[(4-methylphenyl)sulfanyl]pyrimidine-2,4-diamine
6-[4-(2-methylpropyl)phenyl]-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
6-[4-(methanesulfonyl)phenyl]-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
7-(benzyloxy)-1-(3,4-dichlorobenzyl)-1H-benzimidazol-2-amine
-
-
7-chloro-1-(3,4-dichlorobenzyl)-1H-benzimidazol-2-amine
-
-
9-methyl-2-(2-phenylethyl)-9H-purin-6-amine
-
cycloguanil
CYC, the known inhibitor of Plasmodial and Trypanosomal DHFR-TS enzymes is also as an inhibitor of TbPTR1
dihydroneopterin
-
substrate inhibition
Dihydrosepiapterin
-
substrate inhibition
dimethyl 1-[(4-[[3-(ethoxycarbonyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-2,4-dicarboxylate
-
-
dimethyl 1-[(4-[[3-phenyl-7-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-2,4-dicarboxylate
-
-
ethyl 1-[(4-[[7-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-2-carboxylate
methyl 1-[(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]phenyl)carbonyl]piperidine-4-carboxylate
methyl 1-[(4-[[(2,4-diaminopteridin-6-yl)methyl]amino]phenyl)carbonyl]piperidine-4-carboxylate
N,N'-[tridecane-1,13-diylbis[(4,1-phenylene)methylene]]bis[1-(2-methoxyphenyl)methanamine]
-
N-isobutyl-19-(3',4'-methylenedioxyphenyl)-(2E,4E)-nonadecadienamide
-
-
N-[3-(2,4-diamino-5-cyano-7H-pyrrolo[2,3-d]pyrimidin-6-yl)phenyl]methanesulfonamide
-
-
N-[3-(2-amino-5-cyano-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)phenyl]methanesulfonamide
-
-
N-[6-amino-5-(4-methoxyphenyl)-4,4-dimethyl-4,5-dihydrotriazin-2-yl]acetamide
competitive inhibition
-
N1,N1-bis(4-fluorophenyl)-N2-(3-phenylpropyl)ethane-1,2-diamine
-
N4,N4-dimethyl-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
N4,N6-dibenzylpyrimidine-2,4,6-triamine
-
-
N4-benzylpyrimidine-2,4,6-triamine
-
N4-cyclohexyl-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
N4-cyclohexyl-5-(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
-
N4-cyclopropylpyrimidine-2,4,6-triamine
N4-[(4-fluorophenyl)methyl]pyrimidine-2,4,6-triamine
-
N4-[(4-methoxyphenyl)methyl]pyrimidine-2,4,6-triamine
-
N4-[([1,1'-biphenyl]-4-yl)methyl]pyrimidine-2,4,6-triamine
-
pinobanksin-3-o-acetate
-
-
piperlongimin A
-
i.e. (2E)-N-isobutyl-hexadecenamide
piperlongimin B
-
i.e. (2E)-octadecenoylpiperidine
Pteridines
-
and analogs, overview
-
pyrimidine-2,4,6-triamine
quinonoid 6,7-dimethyl-7,8-dihydropterin
quinonoid dihydrobiopterin
sodium antimony gluconate
-
-
(1R,4S,6R)-4-hydroxy-3-methyl-6-(propan-2-yl)cyclohex-2-en-1-yl 5beta,8alpha,10alpha,13alpha-kaura-9(11),16-dien-18-oate
-
-
(1R,4S,6R)-4-hydroxy-3-methyl-6-(propan-2-yl)cyclohex-2-en-1-yl 5beta,8alpha,10alpha,13alpha-kaura-9(11),16-dien-18-oate
-
-
(1R,4S,6R)-4-hydroxy-3-methyl-6-(propan-2-yl)cyclohex-2-en-1-yl 5beta,8alpha,10alpha,13alpha-kaura-9(11),16-dien-18-oate
-
-
(1R,4S,6R)-4-hydroxy-3-methyl-6-(propan-2-yl)cyclohex-2-en-1-yl 5beta,8alpha,10alpha,13alpha-kaura-9(11),16-dien-18-oate
-
-
(1R,4S,6R)-4-hydroxy-3-methyl-6-(propan-2-yl)cyclohex-2-en-1-yl 5beta,8alpha,9beta,10alpha,13alpha-kaur-16-en-18-oate
-
-
(1R,4S,6R)-4-hydroxy-3-methyl-6-(propan-2-yl)cyclohex-2-en-1-yl 5beta,8alpha,9beta,10alpha,13alpha-kaur-16-en-18-oate
-
-
(1R,4S,6R)-4-hydroxy-3-methyl-6-(propan-2-yl)cyclohex-2-en-1-yl 5beta,8alpha,9beta,10alpha,13alpha-kaur-16-en-18-oate
-
-
(1R,4S,6R)-4-hydroxy-3-methyl-6-(propan-2-yl)cyclohex-2-en-1-yl 5beta,8alpha,9beta,10alpha,13alpha-kaur-16-en-18-oate
-
-
(4S)-4-[[(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]phenyl)carbonyl]amino]-5-oxohexanoic acid
-
(4S)-4-[[(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]phenyl)carbonyl]amino]-5-oxohexanoic acid
-
-
1-[(4-[[6-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-4-carboxylic acid
-
1-[(4-[[6-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-4-carboxylic acid
-
-
1-[(4-[[8-amino-3-phenyl-6-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-4-carboxylic acid
-
1-[(4-[[8-amino-3-phenyl-6-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-4-carboxylic acid
-
-
2,4-diaminopyrimidines
-
overview
2,4-diaminopyrimidines
-
-
2-(3,4-dihydroxyphenyl)-3,6-dihydroxy-4H-1-benzopyran-4-one
-
2-(3,4-dihydroxyphenyl)-3,6-dihydroxy-4H-1-benzopyran-4-one
-
2-(3,4-dihydroxyphenyl)-6-hydroxy-2,3-dihydro-4H-1-benzopyran-4-one
-
2-(3,4-dihydroxyphenyl)-6-hydroxy-2,3-dihydro-4H-1-benzopyran-4-one
-
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidine-4-thione
-
-
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidine-4-thione
-
2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
2-amino-4-oxo-6-phenyl-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-4-oxo-6-phenyl-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
2-amino-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
2-amino-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-amino-6-(1,3-benzodioxol-5-yl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-6-(1,3-benzodioxol-5-yl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
2-amino-6-(3-formylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-6-(3-formylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
2-amino-6-(4-ethylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-6-(4-ethylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
2-amino-6-(4-methoxyphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-6-(4-methoxyphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
2-amino-6-bromo-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
-
2-amino-6-bromo-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
22-phenyl[11,21:24,31-terphenyl]-13,15,34-triol
-
-
22-phenyl[11,21:24,31-terphenyl]-13,15,34-triol
-
-
3,6-dihydroxy-2-(3-hydroxyphenyl)-4H-1-benzopyran-4-one
-
3,6-dihydroxy-2-(3-hydroxyphenyl)-4H-1-benzopyran-4-one
-
3alpha-cinnamoyloxy-9beta-hydroxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-cinnamoyloxy-9beta-hydroxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-cinnamoyloxy-9beta-hydroxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-cinnamoyloxy-9beta-hydroxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-cinnamoyloxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-cinnamoyloxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-cinnamoyloxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-cinnamoyloxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-p-coumaroyloxy-9beta-hydroxy-entkaur-16-en-19-oic acid
-
-
3alpha-p-coumaroyloxy-9beta-hydroxy-entkaur-16-en-19-oic acid
-
-
3alpha-p-coumaroyloxy-9beta-hydroxy-entkaur-16-en-19-oic acid
-
-
3alpha-p-coumaroyloxy-9beta-hydroxy-entkaur-16-en-19-oic acid
-
-
3alpha-p-coumaroyloxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-p-coumaroyloxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-p-coumaroyloxy-ent-kaur-16-en-19-oic acid
-
-
3alpha-p-coumaroyloxy-ent-kaur-16-en-19-oic acid
-
-
4-(benzyloxy)pyrimidine-2,6-diamine
LIB_66
-
4-(benzyloxy)pyrimidine-2,6-diamine
LIB_66
-
6,6'-[1,4-phenylenebis(methyleneazanediyl)]bis(N-benzylhexanamide)
-
-
6,6'-[1,4-phenylenebis(methyleneazanediyl)]bis(N-benzylhexanamide)
-
-
6,6'-[methylenebis[(4,1-phenylene)methyleneazanediyl]]bis(N-benzylhexanamide)
-
-
6,6'-[methylenebis[(4,1-phenylene)methyleneazanediyl]]bis(N-benzylhexanamide)
-
-
6,6'-[[1,1'-biphenyl]-4,4'-diylbis(methyleneazanediyl)]bis(N-benzylhexanamide)
-
-
6,6'-[[1,1'-biphenyl]-4,4'-diylbis(methyleneazanediyl)]bis(N-benzylhexanamide)
-
-
6,7-di(propan-2-yl)pteridine-2,4-diamine
-
-
6,7-di(propan-2-yl)pteridine-2,4-diamine
-
6-(benzylsulfanyl)pyrimidine-2,4-diamine
-
-
6-(benzylsulfanyl)pyrimidine-2,4-diamine
-
6-hydroxy-2-(3-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
the compound shows inhibitory activity both against the targeted enzyme and the parasite with a high selectivity and a low toxicity for humans. Only the (R)-isomer binds in the active site, 50% inhibition at 0.05 mM
6-hydroxy-2-(3-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
the compound shows inhibitory activity both against the targeted enzyme and the parasite with a high selectivity and a low toxicity for humans. Only the (R)-isomer binds in the active site, 81% inhibition at 0.05 mM
6-hydroxy-2-(4-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
-
6-hydroxy-2-(4-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
-
6-methyl-7-(propan-2-yl)pteridine-2,4-diamine
-
-
6-methyl-7-(propan-2-yl)pteridine-2,4-diamine
-
6-phenylpteridine-2,4,7-triamine
-
-
6-phenylpteridine-2,4,7-triamine
-
6-[(3aR,9bS)-2,3,3a,9b-tetrahydro[1]benzopyrano[4,3-b]pyrrol-1(4H)-yl]hexan-1-amine
-
-
6-[(3aR,9bS)-2,3,3a,9b-tetrahydro[1]benzopyrano[4,3-b]pyrrol-1(4H)-yl]hexan-1-amine
-
-
6-[(4-methoxybenzyl)sulfanyl]pyrimidine-2,4-diamine
-
-
6-[(4-methoxybenzyl)sulfanyl]pyrimidine-2,4-diamine
-
6-[(4-methoxyphenyl)methoxy]pyrimidine-2,4-diamine
-
-
6-[(4-methoxyphenyl)methoxy]pyrimidine-2,4-diamine
-
-
6-[(4-methylphenyl)sulfanyl]pyrimidine-2,4-diamine
-
-
6-[(4-methylphenyl)sulfanyl]pyrimidine-2,4-diamine
-
9-methyl-2-(2-phenylethyl)-9H-purin-6-amine
-
-
9-methyl-2-(2-phenylethyl)-9H-purin-6-amine
-
-
dihydrobiopterin
-
substrate inhibition above 0.01 mM
dihydrobiopterin
-
substrate inhibition
dihydrobiopterin
-
inhibits the enzyme at high substrate concentrations
dihydrobiopterin
-
substrate inhibition
dihydrobiopterin
-
inhibits the enzyme at high substrate concentrations
dihydrofolate
-
substrate inhibition above 0.005 mM
dihydrofolate
-
substrate inhibition
ethyl 1-[(4-[[7-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-2-carboxylate
-
ethyl 1-[(4-[[7-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-2-carboxylate
-
-
fischericin F
fischericin F is extracted from Ligularia fischeri. Fischericin F has ferulic acid as the main feature, bound to the ent-kaurane skeleton through an ester bond at C14
-
fischericin F
fischericin F is extracted from Ligularia fischeri. Fischericin F has ferulic acid as the main feature, bound to the ent-kaurane skeleton through an ester bond at C14
-
fischericin F
fischericin F is extracted from Ligularia fischeri. Fischericin F has ferulic acid as the main feature, bound to the ent-kaurane skeleton through an ester bond at C14
-
fischericin F
fischericin F is extracted from Ligularia fischeri. Fischericin F has ferulic acid as the main feature, bound to the ent-kaurane skeleton through an ester bond at C14
-
methotrexate
-
methotrexate
antifolate drug
methotrexate
binding structure
methyl 1-[(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]phenyl)carbonyl]piperidine-4-carboxylate
-
methyl 1-[(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]phenyl)carbonyl]piperidine-4-carboxylate
-
-
methyl 1-[(4-[[(2,4-diaminopteridin-6-yl)methyl]amino]phenyl)carbonyl]piperidine-4-carboxylate
-
methyl 1-[(4-[[(2,4-diaminopteridin-6-yl)methyl]amino]phenyl)carbonyl]piperidine-4-carboxylate
-
-
N,N'-[tridecane-1,13-diylbis[(4,1-phenylene)methylene]]bis[1-(2-methoxyphenyl)methanamine]
-
-
N,N'-[tridecane-1,13-diylbis[(4,1-phenylene)methylene]]bis[1-(2-methoxyphenyl)methanamine]
-
-
N1,N1-bis(4-fluorophenyl)-N2-(3-phenylpropyl)ethane-1,2-diamine
-
-
N1,N1-bis(4-fluorophenyl)-N2-(3-phenylpropyl)ethane-1,2-diamine
-
-
N4-benzylpyrimidine-2,4,6-triamine
-
-
N4-benzylpyrimidine-2,4,6-triamine
-
-
N4-cyclopropylpyrimidine-2,4,6-triamine
-
-
N4-cyclopropylpyrimidine-2,4,6-triamine
-
N4-[(4-fluorophenyl)methyl]pyrimidine-2,4,6-triamine
-
-
N4-[(4-fluorophenyl)methyl]pyrimidine-2,4,6-triamine
-
-
N4-[(4-methoxyphenyl)methyl]pyrimidine-2,4,6-triamine
-
-
N4-[(4-methoxyphenyl)methyl]pyrimidine-2,4,6-triamine
-
-
N4-[([1,1'-biphenyl]-4-yl)methyl]pyrimidine-2,4,6-triamine
-
-
N4-[([1,1'-biphenyl]-4-yl)methyl]pyrimidine-2,4,6-triamine
-
-
pyrimethamine
complete inhibition at 0.05 mM
pyrimethamine
complete inhibition at 0.05 mM
pyrimidine-2,4,6-triamine
-
-
pyrimidine-2,4,6-triamine
-
quinonoid 6,7-dimethyl-7,8-dihydropterin
-
-
quinonoid 6,7-dimethyl-7,8-dihydropterin
-
-
quinonoid dihydrobiopterin
-
-
quinonoid dihydrobiopterin
-
-
SANC00368
-
-
SANC00470
-
-
ZINC00057846
-
-
ZINC00359797
-
-
ZINC0058117
i.e. SANC00320, eriodictyol
-
ZINC0058117
i.e. SANC00320, eriodictyol
-
ZINC00612219
-
-
ZINC00630525
-
-
ZINC00677623
-
-
ZINC00809143
-
-
ZINC01003765
-
-
ZINC02177983
-
-
ZINC02184332
-
-
ZINC02690799
-
-
ZINC04313814
-
-
ZINC04523829
-
-
ZINC04671320
-
-
ZINC06556964
-
-
ZINC08992677
-
-
additional information
an in-house database of 360 kauranes (tetracyclic diterpenes) is generated, and a combined ligand- and structure-based virtual screening (VS) approach is performed to select potential inhibitors of Leishmania major (Lm) pteridine reductase I (PTR1). The best-ranked kauranes are employed to verify the validity of the VS approach through LmPTR1 enzyme inhibition assay, molecular dynamics and docking calculations and simulations. Inhibitor synthesis and structure-activity relationship, enzyme-inhibitor interaction analysis using LmPTR1 crystal structure (PDB ID 1E7W) in complex with its respective inhibitor, methotrexate (PDB ID MTX), overview
-
additional information
an in-house database of 360 kauranes (tetracyclic diterpenes) is generated, and a combined ligand- and structure-based virtual screening (VS) approach is performed to select potential inhibitors of Leishmania major (Lm) pteridine reductase I (PTR1). The best-ranked kauranes are employed to verify the validity of the VS approach through LmPTR1 enzyme inhibition assay, molecular dynamics and docking calculations and simulations. Inhibitor synthesis and structure-activity relationship, enzyme-inhibitor interaction analysis using LmPTR1 crystal structure (PDB ID 1E7W) in complex with its respective inhibitor, methotrexate (PDB ID MTX), overview
-
additional information
a Cosseq genome-wide gain of function screen is performed against methotrexate and against the two thymidylate synthase inhibitors 5-fluorouracil and pemetrexed
-
additional information
-
a Cosseq genome-wide gain of function screen is performed against methotrexate and against the two thymidylate synthase inhibitors 5-fluorouracil and pemetrexed
-
additional information
-
-
-
additional information
-
-
-
additional information
-
relatively insensitive to methorexate
-
additional information
structure-based inhibitor development
-
additional information
-
structure-based inhibitor development
-
additional information
-
the enzyme is considered a promising target for anti-leishmanial drug development and several inhibitors that share the substrate scaffold. Design of a series of thiazolidine-2,4-dione derivatives as PTR1 inhibitors by employing the thiazolidinone ring as a bioisosteric replacement for pteridine/purine ring, docking studies, molecular dynamics simulations, and inhibition mechanism, overview
-
additional information
chromen-4-one derivatives as pteridine reductase 1 (PTR1) inhibitors, observed and predicted binding modes of the compounds, docking and modeling, overview. There are differences between the binding modes of the chromen-4-one and the chroman-4-one moiety. No inhibition by 3,6-dihydroxy-2-(4-hydroxyphenyl)-4H-1-benzopyran-4-one at 0.05 mM. Only the (R)-isomers bind in the active site
-
additional information
docking study, structure-function analysis, and drug design. The effects of several factors on docking accuracy, including ligand and protein flexibility, are analyzed
-
additional information
-
docking study, structure-function analysis, and drug design. The effects of several factors on docking accuracy, including ligand and protein flexibility, are analyzed
-
additional information
identification of a 2,4-diaminopyrimidine scaffold targeting Trypanosoma brucei pteridine reductase 1 from the LIBRA compound library screening campaign, screening of the LIBRA compound library against Trypanosoma brucei and Leishmania major pteridine reductase 1, TbPTR1 and LmPTR1, NMR study, overview. Nine compounds are active against parasitic PTR1 and are selected for cell-based parasite screening, as single agents and in combination with methotrexate (MTX). The most interesting TbPTR1 inhibitor identified is 4-(benzyloxy)pyrimidine-2,6-diamine (LIB_66). Subsequently, 6 different LIB_66 derivatives are synthesized to explore its structure-activity relationship (SAR) and absorption, distribution, metabolism, excretion and toxicity (ADMET) properties. The compounds are more inhibitory against the enzyme from Trypanosoma brucei compared to the enzyme from Leishmania major. Docking study and molecular modelling
-
additional information
-
identification of a 2,4-diaminopyrimidine scaffold targeting Trypanosoma brucei pteridine reductase 1 from the LIBRA compound library screening campaign, screening of the LIBRA compound library against Trypanosoma brucei and Leishmania major pteridine reductase 1, TbPTR1 and LmPTR1, NMR study, overview. Nine compounds are active against parasitic PTR1 and are selected for cell-based parasite screening, as single agents and in combination with methotrexate (MTX). The most interesting TbPTR1 inhibitor identified is 4-(benzyloxy)pyrimidine-2,6-diamine (LIB_66). Subsequently, 6 different LIB_66 derivatives are synthesized to explore its structure-activity relationship (SAR) and absorption, distribution, metabolism, excretion and toxicity (ADMET) properties. The compounds are more inhibitory against the enzyme from Trypanosoma brucei compared to the enzyme from Leishmania major. Docking study and molecular modelling
-
additional information
design, docking, and absorption, distribution, metabolism, excretion, and toxicity (ADMET) prediction studies of 2-substituted-5-[(6-substituted-1H-benzimidazol-2yl)methyl]azole derivatives as PTR1 inhibitors. Molecular docking studies using the enzyme crystal structure (PDB ID 1E92) and detailed interaction analysis of compounds with the enzyme, overview. All compounds follow Lipinski's rule of five and can be considered as good oral candidates
-
additional information
in silico identification and in vitro evaluation of natural inhibitors of Leishmania major pteridine reductase I. No inhibition by phillyrin, magnolin, and isosakuranetin. Docking study of inhibitors using the structure of LmPTR1 (PDB ID 2BFM), co-crystallized with NADP+, structure modeling, overview. Apart from salvianolic acid A (5), the most active inhibitors share structural features with certain similarities, such as engaging in Pi-Pi interactions with the nicotinamide moiety, namely, a flavone, a flavonol, a flavanone, or a four-chromanone system
-
additional information
-
in silico identification and in vitro evaluation of natural inhibitors of Leishmania major pteridine reductase I. No inhibition by phillyrin, magnolin, and isosakuranetin. Docking study of inhibitors using the structure of LmPTR1 (PDB ID 2BFM), co-crystallized with NADP+, structure modeling, overview. Apart from salvianolic acid A (5), the most active inhibitors share structural features with certain similarities, such as engaging in Pi-Pi interactions with the nicotinamide moiety, namely, a flavone, a flavonol, a flavanone, or a four-chromanone system
-
additional information
an in-house database of 360 kauranes (tetracyclic diterpenes) is generated, and a combined ligand- and structure-based virtual screening (VS) approach is performed to select potential inhibitors of Leishmania major (Lm) pteridine reductase I (PTR1). The best-ranked kauranes are employed to verify the validity of the VS approach through LmPTR1 enzyme inhibition assay, molecular dynamics and docking calculations and simulations. Inhibitor synthesis and structure-activity relationship, enzyme-inhibitor interaction analysis using LmPTR1 crystal structure (PDB ID 1E7W) in complex with its respective inhibitor, methotrexate (PDB ID MTX), overview
-
additional information
-
an in-house database of 360 kauranes (tetracyclic diterpenes) is generated, and a combined ligand- and structure-based virtual screening (VS) approach is performed to select potential inhibitors of Leishmania major (Lm) pteridine reductase I (PTR1). The best-ranked kauranes are employed to verify the validity of the VS approach through LmPTR1 enzyme inhibition assay, molecular dynamics and docking calculations and simulations. Inhibitor synthesis and structure-activity relationship, enzyme-inhibitor interaction analysis using LmPTR1 crystal structure (PDB ID 1E7W) in complex with its respective inhibitor, methotrexate (PDB ID MTX), overview
-
additional information
an in-house database of 360 kauranes (tetracyclic diterpenes) is generated, and a combined ligand- and structure-based virtual screening (VS) approach is performed to select potential inhibitors of Leishmania major (Lm) pteridine reductase I (PTR1). The best-ranked kauranes are employed to verify the validity of the VS approach through LmPTR1 enzyme inhibition assay, molecular dynamics and docking calculations and simulations. Inhibitor synthesis and structure-activity relationship, enzyme-inhibitor interaction analysis using LmPTR1 crystal structure (PDB ID 1E7W) in complex with its respective inhibitor, methotrexate (PDB ID MTX), overview
-
additional information
-
an in-house database of 360 kauranes (tetracyclic diterpenes) is generated, and a combined ligand- and structure-based virtual screening (VS) approach is performed to select potential inhibitors of Leishmania major (Lm) pteridine reductase I (PTR1). The best-ranked kauranes are employed to verify the validity of the VS approach through LmPTR1 enzyme inhibition assay, molecular dynamics and docking calculations and simulations. Inhibitor synthesis and structure-activity relationship, enzyme-inhibitor interaction analysis using LmPTR1 crystal structure (PDB ID 1E7W) in complex with its respective inhibitor, methotrexate (PDB ID MTX), overview
-
additional information
-
-
-
additional information
-
structure-based design and synthesis of 61 antiparasitic pyrrolopyrimidines targeting pteridine reductase 1, with input from crystal structures of 23 of these compounds complexed with enzyme PTR1, structure-activity relationships, inhibition mechanism, overview. Analysis of eight compounds sufficiently active in vivo evaluation in HEK cells, pharmacokinetic properties
-
additional information
chromen-4-one derivatives as pteridine reductase 1 (PTR1) inhibitors, observed and predicted binding modes of the compounds, docking and modeling, overview. There are differences between the binding modes of the chromen-4-one and the chroman-4-one moiety. No inhibition by 3,6-dihydroxy-2-(4-hydroxyphenyl)-4H-1-benzopyran-4-one at 0.05 mM
-
additional information
monocyclic and bicyclic aromatic systems have been proposed as inhibitors of Trypanosoma brucei PTR1 (TbPTR1), but the size of the catalytic cavity allows the accommodation of expanded molecular cores. Inhibitor development and evaluation, overview
-
additional information
docking study, structure-function analysis, and drug design. The effects of several factors on docking accuracy, including ligand and protein flexibility, are analyzed
-
additional information
identification of a 2,4-diaminopyrimidine scaffold targeting Trypanosoma brucei pteridine reductase 1 from the LIBRA compound library screening campaign, screening of the LIBRA compound library against Trypanosoma brucei and Leishmania major pteridine reductase 1, TbPTR1 and LmPTR1, NMR study, overview. Nine compounds are active against parasitic PTR1 and are selected for cell-based parasite screening, as single agents and in combination with methotrexate (MTX). The most interesting TbPTR1 inhibitor identified is 4-(benzyloxy)pyrimidine-2,6-diamine (LIB_66). Subsequently, 6 different LIB_66 derivatives are synthesized to explore its structure-activity-relationship (SAR) and absorption, distribution, metabolism, excretion and toxicity (ADMET) properties. The compounds are more inhibitory against the enzyme from Trypanosoma brucei compared to the enzyme from Leishmania major. Docking study and molecular modelling; N4,N6-dibenzylpyrimidine-2,4,6-triamine is not inhibitory
-
additional information
successful dual inhibition of Trypanosoma brucei dihydrofolate reductase (TbDHFR, EC 1.5.1.3) and Trypanosoma brucei pteridine reductase 1 (TbPTR1) has implications in the exploitation of anti-folates. Molecular docking of a ligand library of 5742 compounds against TbPTR1 and identification of compounds showing promising binding modes. The protein-ligand complexes are subjected to molecular dynamics to characterize their molecular interactions and energetics, followed by in vitro testing. Five compounds show low micromolar Trypanosome growth inhibition in in vitro experiments that might be acting by inhibition of TbPTR1. Docking study with TbPTR1 and comparison with Trypanosoma cruzi PTR2, molecular dynamics, overview
-
additional information
comparison of the X-ray crystal structure of the TbPTR1:NADP(H):CYC complex (PDB ID 6HNC) with the derivatives' structures 1-(3,4-dichlorophenyl)-6,6-dimethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine (PDB ID 6HNR) and 1-(3,4-dichlorophenyl)-6-(4-nitrophenyl)-1,6-dihydro-1,3,5-triazine-2,4-diamine (PDB ID 6HOW). Selectivity of the ihibitors versus enzymes PTR1 and DHFR, overview
-
additional information
successful dual inhibition of Trypanosoma brucei dihydrofolate reductase (TbDHFR, EC 1.5.1.3) and Trypanosoma brucei pteridine reductase 1 (TbPTR1) has implications in the exploitation of anti-folates. Molecular docking of a ligand library of 5742 compounds against TbPTR1 and identification of compounds showing promising binding modes. The protein-ligand complexes are subjected to molecular dynamics to characterize their molecular interactions and energetics, followed by in vitro testing. Five compounds show low micromolar Trypanosome growth inhibition in in vitro experiments that might be acting by inhibition of TbPTR1. Docking study with TbPTR1 and comparison with Trypanosoma cruzi PTR2, molecular dynamics, overview
-
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.
0.06
(2-amino-2,3-dihydro-1H-benzimidazol-1-yl)(phenyl)methanone
-
Ki above 0.06 mM, pH and temperature not specified in the publication
0.00011 - 0.00018
(4S)-4-[[(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]phenyl)carbonyl]amino]-5-oxohexanoic acid
0.0037
1-(2,5-dichlorobenzyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.01
1-(2-chlorobenzyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.021
1-(2-fluorobenzyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.015
1-(2-methylbenzyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.024
1-(2-phenylethyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.06
1-(3,4-dichlorobenzyl)-1H-benzimidazol-2-amine
-
Ki above 0.06 mM, pH and temperature not specified in the publication
0.0004
1-(3,4-dichlorobenzyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.00046
1-(3,4-dichlorobenzyl)-4-methoxy-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.06
1-(3,4-dichlorobenzyl)-4-phenyl-1H-benzimidazol-2-amine
-
Ki above 0.06 mM, pH and temperature not specified in the publication
0.00031
1-(3,4-dichlorobenzyl)-4-propoxy-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0039
1-(3,4-dichlorobenzyl)-5,6-dimethyl-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.00065
1-(3,4-dichlorobenzyl)-7-methoxy-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.000007
1-(3,4-dichlorobenzyl)-7-phenyl-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.000047
1-(3,4-dichlorobenzyl)-7-propoxy-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0088
1-(3,5-dichlorobenzyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0075
1-(3-chlorobenzyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0031
1-(4-bromobenzyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0054
1-(4-chlorobenzyl)-2,3-dihydro-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.015
1-(4-methylbenzyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0042
1-(4-tert-butylbenzyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0061
1-(naphthalen-1-ylmethyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0028
1-(naphthalen-2-ylmethyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.053
1-(pyridin-2-yl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.054
1-(pyridin-3-yl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.016
1-benzyl-2,3-dihydro-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.2
1-ethyl-2,3-dihydro-1H-benzimidazol-2-amine
-
Ki above 0.2 mM, pH and temperature not specified in the publication
0.007 - 0.075
1-[(4-[[6-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-4-carboxylic acid
0.02
1-[(4-[[8-amino-3-phenyl-6-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-4-carboxylic acid
-
-
0.0063
1-[3-(trifluoromethyl)benzyl]-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.228
1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.003317
2,4-diamino-6-bromo-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH and temperature not specified in the publication
0.00016
2,4-diamino-6-[(E)-2-phenylethenyl]-7H-pyrrolo[2,3-d]-pyrimidine-5-carbonitrile
-
pH and temperature not specified in the publication
0.00035
2,4-diamino-6-[(Z)-2-(4-methylphenyl)ethenyl]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH and temperature not specified in the publication
0.00024
2,4-diamino-6-[(Z)-2-phenylethenyl]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH and temperature not specified in the publication
0.0049
2,4-diamino-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH and temperature not specified in the publication
0.141
2,4-diaminopyrimidine
called compound 3
0.083
2,4-diaminopyrimido[4,5-b]indol-6-ol
pH 5.0, 25°C, recombinant enzyme
-
0.021
2,4-diaminoquinazoline
called compound 2
0.027 - 0.035
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
0.027 - 0.035
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidine-4-thione
0.1
2-amino-4-(cyclopentyloxy)-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
above, pH and temperature not specified in the publication
0.0088
2-amino-4-(thiomorpholin-4-yl)-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH and temperature not specified in the publication
0.075
2-amino-4-methoxy-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
above, pH and temperature not specified in the publication
0.0058 - 0.027
2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
0.00071 - 0.027
2-amino-4-oxo-6-phenyl-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
0.000137
2-amino-4-oxo-6-[(E)-2-phenylethenyl]-4,7-dihydro-3Hpyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH and temperature not specified in the publication
0.1
2-amino-4-[(propan-2-yl)oxy]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
above, pH and temperature not specified in the publication
0.00025
2-amino-5,6-bis(4-chlorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.00076
2-amino-5,6-bis(4-fluorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.002 - 0.01
2-amino-5,6-bis(4-methylphenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.00117
2-amino-5,6-diphenyl-3,7-dihydro-4H-pyrrolo[2,3-d]-pyrimidin-4-one
-
pH and temperature not specified in the publication
0.00027 - 0.027
2-amino-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
0.00047
2-amino-5-(3-chlorophenyl)-6-(4-fluorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.0013
2-amino-5-(4-fluorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.0012
2-amino-5-(4-methylphenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.0073
2-amino-5-methyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.00106
2-amino-5-methyl-6-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.0012
2-amino-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.0004 - 0.0026
2-amino-6-(1,3-benzodioxol-5-yl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
0.0002
2-amino-6-(3-formylphenyl)-4-(1-pyrrolidinyl)-7H-pyrrolo-[2,3-d]pyrimidine-5-carbonitrile
-
pH and temperature not specified in the publication
0.00029 - 0.0042
2-amino-6-(3-formylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
0.00023
2-amino-6-(4-bromophenyl)-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.0005 - 0.0164
2-amino-6-(4-ethylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
0.0005
2-amino-6-(4-fluorophenyl)-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.00036 - 0.0034
2-amino-6-(4-methoxyphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
0.0008
2-amino-6-bromo-4-(1-pyrrolidinyl)-7H-pyrrolo[2,3-d]-pyrimidine-5-carbonitrile
-
pH and temperature not specified in the publication
0.0039 - 0.027
2-amino-6-bromo-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
0.01
2-amino-6-chloro-benzimidazole
-
0.00095
2-amino-6-phenyl-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.000731
2-amino-6-[3-(methanesulfonyl)phenyl]-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH and temperature not specified in the publication
0.01
2-amino-6-[4-(2-methylpropyl)phenyl]-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
above, pH and temperature not specified in the publication
0.01
2-amino-6-[4-[3-(4-morpholinyl)propyl]phenyl]-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one trifluoroacetate
-
above, in Creek's minimal medium, pH and temperature not specified in the publication
0.0057 - 0.01
22-phenyl[11,21:24,31-terphenyl]-13,15,34-triol
-
0.0042
4-(1-pyrrolidinyl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine
-
pH and temperature not specified in the publication
0.000428
4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydro-4H-pyrimidin-5-carboxylic acid ethyl ester
-
pH 4.8, 30°C
0.016
4-(benzyloxy)-1-(3,4-dichlorobenzyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0006 - 0.1
4-(benzyloxy)pyrimidine-2,6-diamine
-
0.0086
4-(thiomorpholin-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine
-
pH and temperature not specified in the publication
0.0023
4-chloro-1-(3,4-dichlorobenzyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0003
5,6-bis(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.00059
5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.00026
5-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.00029
5-(3-chlorophenyl)-6-(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.05
5-(4-fluorophenyl)-4-(2-methylpropoxy)-7H-pyrrolo[2,3-d]pyrimidin-2-amine
-
above, pH and temperature not specified in the publication
0.00048
5-(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.00032
5-(4-methylphenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.00019
5-(phenylethynyl)-4-(1-pyrrolidinyl)-7H-pyrrolo[2,3-d]-pyrimidin-2-amine
-
pH and temperature not specified in the publication
0.0004
5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.0017 - 0.1
6,6'-[1,4-phenylenebis(methyleneazanediyl)]bis(N-benzylhexanamide)
-
0.0027 - 0.0148
6,6'-[methylenebis[(4,1-phenylene)methyleneazanediyl]]bis(N-benzylhexanamide)
-
0.0016 - 0.0192
6,6'-[[1,1'-biphenyl]-4,4'-diylbis(methyleneazanediyl)]bis(N-benzylhexanamide)
-
0.00024 - 0.0033
6,7-di(propan-2-yl)pteridine-2,4-diamine
0.000135
6-(4-bromophenyl)-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.00058
6-(4-fluorophenyl)-5-(4-methoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.0003
6-(4-fluorophenyl)-5-(4-methoxyphenyl)-N4,N4-dimethyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
in Creek's minimal medium, pH and temperature not specified in the publication
0.00024
6-(4-fluorophenyl)-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.0006 - 0.0032
6-(benzylsulfanyl)pyrimidine-2,4-diamine
0.0012 - 0.035
6-methyl-7-(propan-2-yl)pteridine-2,4-diamine
0.0012 - 0.0034
6-phenylpteridine-2,4,7-triamine
0.0016 - 0.1
6-[(3aR,9bS)-2,3,3a,9b-tetrahydro[1]benzopyrano[4,3-b]pyrrol-1(4H)-yl]hexan-1-amine
-
0.0027 - 0.018
6-[(4-methoxybenzyl)sulfanyl]pyrimidine-2,4-diamine
0.0008 - 0.1
6-[(4-methoxyphenyl)methoxy]pyrimidine-2,4-diamine
-
0.0054 - 0.027
6-[(4-methylphenyl)sulfanyl]pyrimidine-2,4-diamine
0.00058
6-[4-(2-methylpropyl)phenyl]-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.00128
6-[4-(methanesulfonyl)phenyl]-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.000098
7-(benzyloxy)-1-(3,4-dichlorobenzyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.00051
7-chloro-1-(3,4-dichlorobenzyl)-1H-benzimidazol-2-amine
-
pH and temperature not specified in the publication
0.0049 - 0.012
9-methyl-2-(2-phenylethyl)-9H-purin-6-amine
-
0.00015 - 0.0038
dihydrobiopterin
0.038
dimethyl 1-[(4-[[3-(ethoxycarbonyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-2,4-dicarboxylate
-
-
0.04
dimethyl 1-[(4-[[3-phenyl-7-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-2,4-dicarboxylate
-
-
0.006 - 0.106
ethyl 1-[(4-[[7-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-2-carboxylate
0.0000111 - 0.000152
methotrexate
0.000037
methyl 1-[(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]phenyl)carbonyl]piperidine-4-carboxylate
-
0.0001 - 0.007
methyl 1-[(4-[[(2,4-diaminopteridin-6-yl)methyl]amino]phenyl)carbonyl]piperidine-4-carboxylate
0.0002 - 0.0372
N,N'-[tridecane-1,13-diylbis[(4,1-phenylene)methylene]]bis[1-(2-methoxyphenyl)methanamine]
-
0.00023
N-[3-(2,4-diamino-5-cyano-7H-pyrrolo[2,3-d]pyrimidin-6-yl)phenyl]methanesulfonamide
-
pH and temperature not specified in the publication
0.00035
N-[3-(2-amino-5-cyano-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)phenyl]methanesulfonamide
-
pH and temperature not specified in the publication
0.0022 - 0.1
N1,N1-bis(4-fluorophenyl)-N2-(3-phenylpropyl)ethane-1,2-diamine
-
0.00029
N4,N4-dimethyl-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
in Creek's minimal medium, pH and temperature not specified in the publication
0.1
N4,N6-dibenzylpyrimidine-2,4,6-triamine
pH 7.4, 25°C
-
0.0034 - 0.1
N4-benzylpyrimidine-2,4,6-triamine
-
0.0002
N4-cyclohexyl-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
in Creek's minimal medium, pH and temperature not specified in the publication
0.00056
N4-cyclohexyl-5-(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
-
pH and temperature not specified in the publication
0.027 - 0.035
N4-cyclopropylpyrimidine-2,4,6-triamine
0.0011 - 0.1
N4-[(4-fluorophenyl)methyl]pyrimidine-2,4,6-triamine
-
0.0003 - 0.0416
N4-[(4-methoxyphenyl)methyl]pyrimidine-2,4,6-triamine
-
0.0002 - 0.0153
N4-[([1,1'-biphenyl]-4-yl)methyl]pyrimidine-2,4,6-triamine
-
0.027 - 0.035
pyrimidine-2,4,6-triamine
0.0922 - 0.475
quinonoid 6,7-dimethyl-7,8-dihydropterin
0.00122 - 0.00314
quinonoid dihydrobiopterin
additional information
additional information
-
0.00011
(4S)-4-[[(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]phenyl)carbonyl]amino]-5-oxohexanoic acid
-
-
0.00018
(4S)-4-[[(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]phenyl)carbonyl]amino]-5-oxohexanoic acid
-
0.007
1-[(4-[[6-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-4-carboxylic acid
-
0.075
1-[(4-[[6-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-4-carboxylic acid
-
-
0.027
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH 7.5, temperature not specified in the publication, value above 0.027
0.035
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
pH 7.5, temperature not specified in the publication, value above 0.035
0.027
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidine-4-thione
-
pH 7.5, temperature not specified in the publication, value above 0.027
0.035
2-amino-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidine-4-thione
pH 7.5, temperature not specified in the publication, value above 0.035
0.0058
2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
pH 7.5, temperature not specified in the publication
0.027
2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH 7.5, temperature not specified in the publication, value above 0.027
0.00071
2-amino-4-oxo-6-phenyl-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
pH 7.5, temperature not specified in the publication
0.027
2-amino-4-oxo-6-phenyl-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH 7.5, temperature not specified in the publication, value above 0.027
0.00027
2-amino-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH and temperature not specified in the publication
0.00096
2-amino-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
pH 7.5, temperature not specified in the publication
0.027
2-amino-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
pH 7.5, temperature not specified in the publication, value above 0.027
0.0004
2-amino-6-(1,3-benzodioxol-5-yl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
pH 7.5, temperature not specified in the publication
0.0026
2-amino-6-(1,3-benzodioxol-5-yl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH 7.5, temperature not specified in the publication
0.00029
2-amino-6-(3-formylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
pH 7.5, temperature not specified in the publication
0.0042
2-amino-6-(3-formylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH 7.5, temperature not specified in the publication
0.0005
2-amino-6-(4-ethylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
pH 7.5, temperature not specified in the publication
0.0164
2-amino-6-(4-ethylphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH 7.5, temperature not specified in the publication
0.00036
2-amino-6-(4-methoxyphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
pH 7.5, temperature not specified in the publication
0.0034
2-amino-6-(4-methoxyphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH 7.5, temperature not specified in the publication
0.0039
2-amino-6-bromo-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
pH 7.5, temperature not specified in the publication
0.027
2-amino-6-bromo-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
-
pH 7.5, temperature not specified in the publication, value above 0.027
0.0057
22-phenyl[11,21:24,31-terphenyl]-13,15,34-triol
pH 7.4, 25°C
-
0.01
22-phenyl[11,21:24,31-terphenyl]-13,15,34-triol
pH 7.4, 25°C
-
0.0006
4-(benzyloxy)pyrimidine-2,6-diamine
pH 7.4, 25°C
-
0.1
4-(benzyloxy)pyrimidine-2,6-diamine
pH 7.4, 25°C
-
0.0017
6,6'-[1,4-phenylenebis(methyleneazanediyl)]bis(N-benzylhexanamide)
pH 7.4, 25°C
-
0.1
6,6'-[1,4-phenylenebis(methyleneazanediyl)]bis(N-benzylhexanamide)
pH 7.4, 25°C
-
0.0027
6,6'-[methylenebis[(4,1-phenylene)methyleneazanediyl]]bis(N-benzylhexanamide)
pH 7.4, 25°C
-
0.0148
6,6'-[methylenebis[(4,1-phenylene)methyleneazanediyl]]bis(N-benzylhexanamide)
pH 7.4, 25°C
-
0.0016
6,6'-[[1,1'-biphenyl]-4,4'-diylbis(methyleneazanediyl)]bis(N-benzylhexanamide)
pH 7.4, 25°C
-
0.0192
6,6'-[[1,1'-biphenyl]-4,4'-diylbis(methyleneazanediyl)]bis(N-benzylhexanamide)
pH 7.4, 25°C
-
0.00024
6,7-di(propan-2-yl)pteridine-2,4-diamine
-
pH 7.5, temperature not specified in the publication
0.0033
6,7-di(propan-2-yl)pteridine-2,4-diamine
pH 7.5, temperature not specified in the publication
0.0006
6-(benzylsulfanyl)pyrimidine-2,4-diamine
-
pH 7.5, temperature not specified in the publication
0.0032
6-(benzylsulfanyl)pyrimidine-2,4-diamine
pH 7.5, temperature not specified in the publication
0.0012
6-methyl-7-(propan-2-yl)pteridine-2,4-diamine
-
pH 7.5, temperature not specified in the publication
0.035
6-methyl-7-(propan-2-yl)pteridine-2,4-diamine
pH 7.5, temperature not specified in the publication, value above 0.035
0.0012
6-phenylpteridine-2,4,7-triamine
pH 7.5, temperature not specified in the publication
0.0034
6-phenylpteridine-2,4,7-triamine
-
pH 7.5, temperature not specified in the publication
0.0016
6-[(3aR,9bS)-2,3,3a,9b-tetrahydro[1]benzopyrano[4,3-b]pyrrol-1(4H)-yl]hexan-1-amine
pH 7.4, 25°C
-
0.1
6-[(3aR,9bS)-2,3,3a,9b-tetrahydro[1]benzopyrano[4,3-b]pyrrol-1(4H)-yl]hexan-1-amine
pH 7.4, 25°C
-
0.0027
6-[(4-methoxybenzyl)sulfanyl]pyrimidine-2,4-diamine
-
pH 7.5, temperature not specified in the publication
0.018
6-[(4-methoxybenzyl)sulfanyl]pyrimidine-2,4-diamine
pH 7.5, temperature not specified in the publication
0.0008
6-[(4-methoxyphenyl)methoxy]pyrimidine-2,4-diamine
pH 7.4, 25°C
-
0.1
6-[(4-methoxyphenyl)methoxy]pyrimidine-2,4-diamine
pH 7.4, 25°C
-
0.0054
6-[(4-methylphenyl)sulfanyl]pyrimidine-2,4-diamine
pH 7.5, temperature not specified in the publication
0.027
6-[(4-methylphenyl)sulfanyl]pyrimidine-2,4-diamine
-
pH 7.5, temperature not specified in the publication, value above 0.027
0.0049
9-methyl-2-(2-phenylethyl)-9H-purin-6-amine
pH 7.4, 25°C
-
0.012
9-methyl-2-(2-phenylethyl)-9H-purin-6-amine
pH 7.4, 25°C
-
0.00015
dihydrobiopterin
-
in 50 mM HEPES buffer, pH 7.4, at 25°C
0.00116
dihydrobiopterin
-
in 50 mM HEPES buffer, pH 7.4, at 25°C
0.0038
dihydrobiopterin
-
pH 3.7
0.006
ethyl 1-[(4-[[7-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-2-carboxylate
-
0.106
ethyl 1-[(4-[[7-(trifluoromethyl)quinoxalin-2-yl]amino]phenyl)carbonyl]piperidine-2-carboxylate
-
-
0.0000111
methotrexate
-
0.000039
methotrexate
pH and temperature not specified in the publication
0.000152
methotrexate
-
pH 3.7
0.0001
methyl 1-[(4-[[(2,4-diaminopteridin-6-yl)methyl]amino]phenyl)carbonyl]piperidine-4-carboxylate
-
0.007
methyl 1-[(4-[[(2,4-diaminopteridin-6-yl)methyl]amino]phenyl)carbonyl]piperidine-4-carboxylate
-
-
0.0002
N,N'-[tridecane-1,13-diylbis[(4,1-phenylene)methylene]]bis[1-(2-methoxyphenyl)methanamine]
pH 7.4, 25°C
-
0.0372
N,N'-[tridecane-1,13-diylbis[(4,1-phenylene)methylene]]bis[1-(2-methoxyphenyl)methanamine]
pH 7.4, 25°C
-
0.0022
N1,N1-bis(4-fluorophenyl)-N2-(3-phenylpropyl)ethane-1,2-diamine
pH 7.4, 25°C
-
0.1
N1,N1-bis(4-fluorophenyl)-N2-(3-phenylpropyl)ethane-1,2-diamine
pH 7.4, 25°C
-
0.0034
N4-benzylpyrimidine-2,4,6-triamine
pH 7.4, 25°C
-
0.1
N4-benzylpyrimidine-2,4,6-triamine
pH 7.4, 25°C
-
0.027
N4-cyclopropylpyrimidine-2,4,6-triamine
-
pH 7.5, temperature not specified in the publication, value above 0.027
0.035
N4-cyclopropylpyrimidine-2,4,6-triamine
pH 7.5, temperature not specified in the publication, value above 0.035
0.0011
N4-[(4-fluorophenyl)methyl]pyrimidine-2,4,6-triamine
pH 7.4, 25°C
-
0.1
N4-[(4-fluorophenyl)methyl]pyrimidine-2,4,6-triamine
pH 7.4, 25°C
-
0.0003
N4-[(4-methoxyphenyl)methyl]pyrimidine-2,4,6-triamine
pH 7.4, 25°C
-
0.0416
N4-[(4-methoxyphenyl)methyl]pyrimidine-2,4,6-triamine
pH 7.4, 25°C
-
0.0002
N4-[([1,1'-biphenyl]-4-yl)methyl]pyrimidine-2,4,6-triamine
pH 7.4, 25°C
-
0.0153
N4-[([1,1'-biphenyl]-4-yl)methyl]pyrimidine-2,4,6-triamine
pH 7.4, 25°C
-
0.027
pyrimidine-2,4,6-triamine
-
pH 7.5, temperature not specified in the publication, value above 0.027
0.035
pyrimidine-2,4,6-triamine
pH 7.5, temperature not specified in the publication, value above 0.035
0.0922
quinonoid 6,7-dimethyl-7,8-dihydropterin
-
in 50 mM HEPES buffer, pH 7.4, at 25°C
0.475
quinonoid 6,7-dimethyl-7,8-dihydropterin
-
in 50 mM HEPES buffer, pH 7.4, at 25°C
0.00122
quinonoid dihydrobiopterin
-
in 50 mM HEPES buffer, pH 7.4, at 25°C
0.00314
quinonoid dihydrobiopterin
-
in 50 mM HEPES buffer, pH 7.4, at 25°C
additional information
additional information
-
inhibition kinetics, thermal shift assay
-
additional information
additional information
all the investigated molecules are assumed to act as full competitive inhibitor and analysed according to the non-tight binding Michaelis-Menten model
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
23.1 - 101
(4-fluoro-phenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydro-pyrimidine-5-carboxylic acid ethyl ester
0.000692
1-(3,4-dichlorophenyl)-6,6-dimethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine
Trypanosoma brucei brucei
pH 3.7, 22°C, recombinant enzyme
0.000186
1-(3,4-dichlorophenyl)-6-(4-nitrophenyl)-1,6-dihydro-1,3,5-triazine-2,4-diamine
Trypanosoma brucei brucei
pH 3.7, 22°C, recombinant enzyme
-
0.00602
1-(4-chlorophenyl)-6-methyl-1,6-dihydro-1,3,5-triazine-2,4-diamine
Trypanosoma brucei brucei
pH 3.7, 22°C, recombinant enzyme
-
0.0275
1-(4-chlorophenyl)-6-propyl-1,6-dihydro-1,3,5-triazine-2,4-diamine
Trypanosoma brucei brucei
pH 3.7, 22°C, recombinant enzyme
-
0.00067
1-(4-methoxyphenyl)-6,6-dimethyl-1,6-dihydro-1,3,5-triazine-2,4-diamine
Trypanosoma brucei brucei
pH 3.7, 22°C, recombinant enzyme
-
0.0624
2,4-diamino-6-bromo-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.07252
2,4-diamino-6-[(E)-2-phenylethenyl]-7H-pyrrolo[2,3-d]-pyrimidine-5-carbonitrile
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.01708
2,4-diamino-6-[(Z)-2-(4-methylphenyl)ethenyl]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.17
2,4-diamino-6-[(Z)-2-phenylethenyl]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
Trypanosoma brucei
-
pH and temperature not specified in the publication
2.44
2,4-diamino-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
Trypanosoma brucei
-
pH and temperature not specified in the publication
18.3 - 90.8
2,6-dimethyl [3-O-benzyl-1,2-O isopropylidene-beta-L-threo-pentofuronose-4-yl]-1-phenyl-1,4-dihydro pyridine-3,5-dicarboxylic acid diethyl ether
0.035 - 0.038
2-(3,4-dihydroxyphenyl)-3,6-dihydroxy-4H-1-benzopyran-4-one
0.036 - 0.082
2-(3,4-dihydroxyphenyl)-6-hydroxy-2,3-dihydro-4H-1-benzopyran-4-one
0.34
2-amino-4-(1-pyrrolidinyl)-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00104
2-amino-4-(cyclopentyloxy)-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
Trypanosoma brucei
-
above, pH and temperature not specified in the publication
0.01433
2-amino-4-(thiomorpholin-4-yl)-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.0073
2-amino-4-[(propan-2-yl)oxy]-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
Trypanosoma brucei
-
above, pH and temperature not specified in the publication
0.00156
2-amino-5,6-bis(4-chlorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00074
2-amino-5,6-bis(4-fluorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00043
2-amino-5,6-bis(4-methylphenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00041
2-amino-5,6-diphenyl-3,7-dihydro-4H-pyrrolo[2,3-d]-pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
7.62
2-amino-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00077
2-amino-5-(3-chlorophenyl)-6-(4-fluorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.02511
2-amino-5-(4-fluorophenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.125
2-amino-5-(4-methylphenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.0104
2-amino-5-methyl-6-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.05334
2-amino-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00775
2-amino-6-(3-formylphenyl)-4-(1-pyrrolidinyl)-7H-pyrrolo-[2,3-d]pyrimidine-5-carbonitrile
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.0032
2-amino-6-(4-bromophenyl)-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00103
2-amino-6-(4-fluorophenyl)-5-(4-methoxyphenyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00061
2-amino-6-(4-fluorophenyl)-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.139
2-amino-6-bromo-4-(1-pyrrolidinyl)-7H-pyrrolo[2,3-d]-pyrimidine-5-carbonitrile
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00014
2-amino-6-phenyl-5-(2-phenylethyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00213
2-amino-6-[4-(2-methylpropyl)phenyl]-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
above, pH and temperature not specified in the publication
0.1
2-amino-6-[4-(methanesulfonyl)phenyl]-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Trypanosoma brucei
-
above, pH and temperature not specified in the publication
0.0201
2-amino-6-[4-[3-(4-morpholinyl)propyl]phenyl]-5-phenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one trifluoroacetate
Trypanosoma brucei
-
above, in Creek's minimal medium, pH and temperature not specified in the publication
0.0043 - 0.0125
3,6-dihydroxy-2-(3-hydroxyphenyl)-4H-1-benzopyran-4-one
0.01
4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydro-4H-pyrimidin-5-carboxylic acid ethyl ester
Leishmania donovani
-
pH 4.8, 30°C
0.0041
4-(4,6-diamino-2,2-dimethyl-1,3,5-triazin-1(2H)-yl)phenol
Trypanosoma brucei brucei
pH 3.7, 22°C, recombinant enzyme
-
0.08006
4-(thiomorpholin-4-yl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00202
5,6-bis(4-chlorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00308
5,6-bis(4-chlorophenyl)-N~4~,N~4~-dimethyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
in Creek's minimal medium, pH and temperature not specified in the publication
0.00015
5,6-bis(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00131
5,6-bis(4-fluorophenyl)-N~4~,N~4~-dimethyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00019
5,6-bis(4-methylphenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00058
5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.09352
5-(2-phenylethyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00019
5-(3-chlorophenyl)-6-(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00122
5-(4-chlorophenyl)-1,3,5-triazaspiro[5.5]undeca-1,3-diene-2,4-diamine
Trypanosoma brucei brucei
pH 3.7, 22°C, recombinant enzyme
-
0.00253
5-(4-fluorophenyl)-4-(2-methylpropoxy)-7H-pyrrolo[2,3-d]pyrimidin-2-amine
Trypanosoma brucei
-
above, pH and temperature not specified in the publication
0.00142
5-(4-fluorophenyl)-4-isopropyloxy-7H-pyrrolo[2,3-d]-pyrimidin-2-amine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.01447
5-(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.17
5-(4-methylphenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00065
5-(phenylethynyl)-4-(1-pyrrolidinyl)-7H-pyrrolo[2,3-d]-pyrimidin-2-amine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.04101
5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00025
6-(4-bromophenyl)-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.000083
6-(4-fluorophenyl)-5-(4-methoxyphenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00343
6-(4-fluorophenyl)-5-(4-methoxyphenyl)-N4,N4-dimethyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
in Creek's minimal medium, pH and temperature not specified in the publication
0.00008
6-(4-fluorophenyl)-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00134
6-(4-fluorophenyl)-N~4~,N~4~-dimethyl-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
in Creek's minimal medium, pH and temperature not specified in the publication
0.031 - 0.057
6-hydroxy-2-(3-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
0.035 - 0.133
6-hydroxy-2-(4-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
0.00139
6-[4-(2-methylpropyl)phenyl]-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00616
6-[4-(methanesulfonyl)phenyl]-5-phenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.0316
cycloguanil
Trypanosoma brucei brucei
pH 3.7, 22°C
0.000793
methotrexate
Trypanosoma brucei brucei
pH 3.7, 22°C
0.00603
N-[3-(2,4-diamino-5-cyano-7H-pyrrolo[2,3-d]pyrimidin-6-yl)phenyl]methanesulfonamide
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00083
N-[6-amino-5-(4-methoxyphenyl)-4,4-dimethyl-4,5-dihydrotriazin-2-yl]acetamide
Trypanosoma brucei brucei
pH 3.7, 22°C, recombinant enzyme
-
0.00611
N4,N4-dimethyl-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
in Creek's minimal medium, pH and temperature not specified in the publication
0.00178
N4-cyclohexyl-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
in Creek's minimal medium, pH and temperature not specified in the publication
0.0115
N~4~-cyclohexyl-5-(4-fluorophenyl)-7H-pyrrolo[2,3-d]pyrimidine-2,4-diamine
Trypanosoma brucei
-
pH and temperature not specified in the publication
0.00009
pyrimethamine
Trypanosoma brucei brucei
pH 3.7, 22°C
12.1
sodium antimony gluconate
Leishmania donovani
-
amastigote
23.1
(4-fluoro-phenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydro-pyrimidine-5-carboxylic acid ethyl ester
Leishmania donovani
-
amastigote
101
(4-fluoro-phenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydro-pyrimidine-5-carboxylic acid ethyl ester
Leishmania donovani
-
promastigote
18.3
2,6-dimethyl [3-O-benzyl-1,2-O isopropylidene-beta-L-threo-pentofuronose-4-yl]-1-phenyl-1,4-dihydro pyridine-3,5-dicarboxylic acid diethyl ether
Leishmania donovani
-
amastigote
90.8
2,6-dimethyl [3-O-benzyl-1,2-O isopropylidene-beta-L-threo-pentofuronose-4-yl]-1-phenyl-1,4-dihydro pyridine-3,5-dicarboxylic acid diethyl ether
Leishmania donovani
-
promastigote
0.035
2-(3,4-dihydroxyphenyl)-3,6-dihydroxy-4H-1-benzopyran-4-one
Leishmania major
pH 6.0, 30°C
0.038
2-(3,4-dihydroxyphenyl)-3,6-dihydroxy-4H-1-benzopyran-4-one
Trypanosoma brucei
pH 6.0, 30°C
0.036
2-(3,4-dihydroxyphenyl)-6-hydroxy-2,3-dihydro-4H-1-benzopyran-4-one
Leishmania major
pH 6.0, 30°C
0.082
2-(3,4-dihydroxyphenyl)-6-hydroxy-2,3-dihydro-4H-1-benzopyran-4-one
Trypanosoma brucei
pH 6.0, 30°C
0.0043
3,6-dihydroxy-2-(3-hydroxyphenyl)-4H-1-benzopyran-4-one
Trypanosoma brucei
pH 6.0, 30°C
0.0125
3,6-dihydroxy-2-(3-hydroxyphenyl)-4H-1-benzopyran-4-one
Leishmania major
pH 6.0, 30°C
0.031
6-hydroxy-2-(3-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
Trypanosoma brucei
pH 6.0, 30°C
0.057
6-hydroxy-2-(3-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
Leishmania major
pH 6.0, 30°C
0.035
6-hydroxy-2-(4-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
Leishmania major
pH 6.0, 30°C
0.133
6-hydroxy-2-(4-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one
Trypanosoma brucei
pH 6.0, 30°C
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.
evolution
PTR1 is a NADPH-dependent enzyme belonging to the short-chain dehydrogenase/reductase (SDR) family
evolution
PTR1 is a short-chain dehydrogenase reductase family member. The trypanosomatid PTR1s are structurally very similar, sequence comparisons
evolution
PTR2 is a short-chain dehydrogenase reductase family member. In Trypanosoma cruzi, TcPTR1 and TcPTR2 are isoforms that show very high sequence homology but also display varied enzymatic activity. TcPTR1 in comparison to TcPTR2 shows higher activity with biopterin and folate than with H2F or H2B
evolution
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
evolution
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
evolution
-
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
-
evolution
-
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
-
malfunction
-
comparisons of isogenic lines shows that ptr1-null mutants are 18fold more sensitive to H2O2 than PTR1-overproducing lines, and significant 3-5fold differences are seen with a broad panel of oxidant-inducing agents
malfunction
-
impossible to generate PTR1 null mutants. RNA interference results in complete knockdown of endogenous protein after 48 h, followed by cell death after 4 days. Lethal phenotype is reversed by expression of PTR1 in RNAi lines or by addition of tetrahydrobiopterin to cultures. Loss of PTR1 is associated with gross morphological changes due to a defect in cytokinesis, resulting in cells with multiple nuclei and kinetoplasts, as well as multiple detached flagella. Electron microscopy also reveal increased numbers of glycosomes, while immunofluorescence microscopy show increased and more diffuse staining for glycosomal matrix enzymes, indicative of mis-localisation to the cytosol. RNAi cell lines are markedly less virulent than wild-type parasites in mice
malfunction
Leishmania can survive without copies of either DHFR-TS or PTR1 but not without both. Leishmania is pterin auxotroph but a PTR1 knockout cell will grow well if sufficient reduced pterins are available
malfunction
the mutant DELTApruA strain exhibits elevated biofilm formation and abundant polysaccharide production independent of surface contact. The plasmid-borne expression of wild-type PruA fully corrects this deficiency, while a plasmid-encoded PruA Y163A mutant variant expressed in the DELTApruA strain has no effect on these DELTApruA mutant phenotypes, with its phenotype appearing similar to the phenotype of the deletion strain alone
malfunction
-
Leishmania can survive without copies of either DHFR-TS or PTR1 but not without both. Leishmania is pterin auxotroph but a PTR1 knockout cell will grow well if sufficient reduced pterins are available
-
malfunction
-
the mutant DELTApruA strain exhibits elevated biofilm formation and abundant polysaccharide production independent of surface contact. The plasmid-borne expression of wild-type PruA fully corrects this deficiency, while a plasmid-encoded PruA Y163A mutant variant expressed in the DELTApruA strain has no effect on these DELTApruA mutant phenotypes, with its phenotype appearing similar to the phenotype of the deletion strain alone
-
malfunction
-
the mutant DELTApruA strain exhibits elevated biofilm formation and abundant polysaccharide production independent of surface contact. The plasmid-borne expression of wild-type PruA fully corrects this deficiency, while a plasmid-encoded PruA Y163A mutant variant expressed in the DELTApruA strain has no effect on these DELTApruA mutant phenotypes, with its phenotype appearing similar to the phenotype of the deletion strain alone
-
metabolism
folates are reduced in Leishmania by the bifunctional dihydrofolate reductase thymidylate synthase (DHFR-TS) and by pteridine reductase (PTR1)
metabolism
key enzymes involved in trypanosome folate metabolism are dihydrofolate reductase (DHFR) and pteridine reductase (PTR1)
metabolism
key enzymes involved in trypanosome folate metabolism are dihydrofolate reductase (DHFR) and pteridine reductase (PTR1)
metabolism
traditional antifolates, such as methotrexate (MTX) inhibiting DHFR, are poorly effective towards trypanosome parasites because of the metabolic bypass provided by PTR1 also catalyzing folate reduction in addition to the conversion of biopterin to 7,8-dihydrobiopterin (DHB) and subsequently to 5,6,7,8-tetrahydrobiopterin (THB)
metabolism
-
folates are reduced in Leishmania by the bifunctional dihydrofolate reductase thymidylate synthase (DHFR-TS) and by pteridine reductase (PTR1)
-
physiological function
-
using treatment with H2O2 as the selective pressure PTR1 is identified as a mediator of susceptibility to oxidative stress. Oxidant resistance depends upon reduced unconjugated pteridines and PTR1-derived pteridines can modulate oxidant susceptibility
physiological function
-
the enzyme has an essential and dual role in pterin metabolism
physiological function
-
the enzyme has an essential and dual role in pterin metabolism
physiological function
the enzyme is able to reduce both unconjugated and conjugated pterins and provides a metabolic bypass to alleviate a dihydrofolate reductase inhibition
physiological function
the enzyme is able to reduce both unconjugated and conjugated pterins and provides a metabolic bypass to alleviate a dihydrofolate reductase inhibition
physiological function
the enzyme participates in the salvage of pteridines, which are essential to maintain growth of Leishmania
physiological function
the enzyme participates in the salvage of pteridines, which are essential to maintain growth of Leishmania
physiological function
the enzyme participates in the salvage of pteridines, which are essential to maintain growth of Leishmania
physiological function
the enzyme participates in the salvage of pteridines, which are essential to maintain growth of Leishmania
physiological function
biofilms are complex multicellular communities that are formed by diverse bacteria. In the plant pathogen Agrobacterium tumefaciens, the transition from a free-living motile state to a nonmotile biofilm state is governed by a novel signaling pathway involving small molecules called pterins. Involvement of pterins in biofilm formation. PruA pteridine reductase is involved in the signaling pathway. The enzymatic activity of PruA is essential for the proposed pterin-dependent regulatory pathway. Wild-type Agrobacterium tumefaciens exhibits basal levels of biofilm formation in laboratory culture and forms pale orange or white colonies when grown on solid growth medium supplemented with Congo red. PruA is an important factor in controlling the motile-to-sessile transition in Agrobacterium tumefaciens
physiological function
in addition to folate reduction, PTR1 also catalyzes the conversion of biopterin to 7,8-dihydrobiopterin (DHB) and subsequently to 5,6,7,8-tetrahydrobiopterin (THB). Under dihydrofolate reductase (DHFR, EC 1.5.1.3) inhibition, PTR1 is upregulated providing reduced folates necessary for parasite survival
physiological function
pteridine reductase 1 (PTR1) has the ability to catalyze the NADPH-dependent two-stage reduction of biopterins to their 7,8-dihydro and 5,6,7,8-tetrahydro forms as well as folates to their H2F and H4F forms. PTR1 is a trypanosomatid multifunctional enzyme that provides a mechanism for escape of dihydrofolate reductase (DHFR, EC 1.5.1.3) inhibition. This is because PTR1 can reduce pterins and folates. Trypanosomes require folates and pterins for survival and are unable to synthesize them de novo
physiological function
pteridine reductase 1 (PTR1, EC 1.5.1.33) has the ability to catalyze the NADPH-dependent two-stage reduction of biopterins to their 7,8-dihydro and 5,6,7,8-tetrahydro forms as well as folates to their H2F and H4F forms. PTR1 is a trypanosomatid multifunctional enzyme that provides a mechanism for escape of dihydrofolate reductase (DHFR) inhibition. This is because PTR1 can reduce pterins and folates. Trypanosomes require folates and pterins for survival and are unable to synthesize them de novo. In Trypanosoma cruzi, TcPTR1 and TcPTR2 are isoforms that show very high sequence homology but also display varied enzymatic activity. TcPTR1 in comparison to TcPTR2 shows higher activity with biopterin and folate than with dihydrofolate or dihydrobiopterin
physiological function
PTR1 is essential in the absence of an intact bifunctional dihydrofolate reductase thymidylate synthase (DHFR-TS) even in the presence of flavin-dependent bacterial TS gene ThyX or thymidine supplementation, indicating the essential role of reduced pterins or folate beyond thymidine synthesis
physiological function
PTR1 produces tetrahydrobiopterin (H4BPt) from dihydrobiopterin (H2BPt) or from fully oxidized biopterin (BPt) scavenged from host cells
physiological function
the enzyme plays a critical role in the pterin metabolic pathway that is absolutely essential for the parasite's survival in the human host
physiological function
the enzyme plays a critical role in the pterin metabolic pathway that is absolutely essential for the parasite's survival in the human host
physiological function
-
PTR1 is essential in the absence of an intact bifunctional dihydrofolate reductase thymidylate synthase (DHFR-TS) even in the presence of flavin-dependent bacterial TS gene ThyX or thymidine supplementation, indicating the essential role of reduced pterins or folate beyond thymidine synthesis
-
physiological function
-
biofilms are complex multicellular communities that are formed by diverse bacteria. In the plant pathogen Agrobacterium tumefaciens, the transition from a free-living motile state to a nonmotile biofilm state is governed by a novel signaling pathway involving small molecules called pterins. Involvement of pterins in biofilm formation. PruA pteridine reductase is involved in the signaling pathway. The enzymatic activity of PruA is essential for the proposed pterin-dependent regulatory pathway. Wild-type Agrobacterium tumefaciens exhibits basal levels of biofilm formation in laboratory culture and forms pale orange or white colonies when grown on solid growth medium supplemented with Congo red. PruA is an important factor in controlling the motile-to-sessile transition in Agrobacterium tumefaciens
-
physiological function
-
biofilms are complex multicellular communities that are formed by diverse bacteria. In the plant pathogen Agrobacterium tumefaciens, the transition from a free-living motile state to a nonmotile biofilm state is governed by a novel signaling pathway involving small molecules called pterins. Involvement of pterins in biofilm formation. PruA pteridine reductase is involved in the signaling pathway. The enzymatic activity of PruA is essential for the proposed pterin-dependent regulatory pathway. Wild-type Agrobacterium tumefaciens exhibits basal levels of biofilm formation in laboratory culture and forms pale orange or white colonies when grown on solid growth medium supplemented with Congo red. PruA is an important factor in controlling the motile-to-sessile transition in Agrobacterium tumefaciens
-
additional information
-
organization of the TbPTR1 active site, overview
additional information
active site structure of TbPTR1, overview
additional information
active-site structure analysis using computational docking and virtual screening techniques. Active site structure comparisons of Tb-PR (PDB ID 3JQ9) with Leishmania major pteridine reductase (Lm-PR). The size of substrate binding cleft is reduced in TbPTR1 due to differences in specific amino acids, the presence of Trp221, adjustment of the beta6-alpha6 loop. Formation of the triad is due to the presence of Cys168, C-terminal carboxyl group and His267 in TbPTR1, detailed overview
additional information
active-site structure analysis using computational docking and virtual screening techniques. Active site structure comparisons of Trypanosoma brucei pteridine reductase Tb-PR (PDB ID 3JQ9) with Lm-PR. The size of substrate binding cleft is reduced in TbPTR1 due to differences in specific amino acids, the presence of Trp221, adjustment of the beta6-alpha6 loop. Formation of the triad is due to the presence of Cys168, C-terminal carboxyl group and His267 in TbPTR1, detailed overview
additional information
-
active-site structure analysis using computational docking and virtual screening techniques. Active site structure comparisons of Trypanosoma brucei pteridine reductase Tb-PR (PDB ID 3JQ9) with Lm-PR. The size of substrate binding cleft is reduced in TbPTR1 due to differences in specific amino acids, the presence of Trp221, adjustment of the beta6-alpha6 loop. Formation of the triad is due to the presence of Cys168, C-terminal carboxyl group and His267 in TbPTR1, detailed overview
additional information
enzyme structure modelling, residue Y163 is involved in catalysis
additional information
hybrid models of LaPTR1
additional information
hybrid models of LbPTR1
additional information
hybrid models of LpPTR1
additional information
-
hybrid models of LpPTR1
additional information
isozyme TcPTR1 has no crystal structure, so for this study a structure is calculated using homology modeling with TcPTR2 as a template
additional information
pterin and folate substrates, along with inhibitors, interact with PTR1 complexes quite similarly, often via binding in a Pi-sandwich between the NADPH nicotinamide ring and residue Phe97. The NADPH cofactor is known to be essential in creating both the substrate binding site as well as the catalytic center. Arg14, Ser95, Phe97, Asp161, and Tyr174 are important residues that interact with the folate and pterin substrates
additional information
the critical proton donor in the reaction is a tyrosine residue which is part of a highly conserved YX3K motif, Tyr 194 and Lys 198 in Leishmania major PTR1
additional information
the substrate-binding domain of LmPTR1 is characterized by a considerable degree of lipophilicity, especially in a part mainly made up by hydrophobic amino acids like Tyr, Phe, Leu, or Val. The NADPH/NADP+-binding part of the catalytic site, on the other hand, is characterized by more hydrophilic amino acids and more polar properties overall. Due to the close vicinity of the co-substrate and substrate binding sites, the co-substrate NADPH/NADP+ may also contribute to the properties of the substrate cavity, introducing the possibility of polar interactions with a ligand bound in the folic acid binding site
additional information
-
the substrate-binding domain of LmPTR1 is characterized by a considerable degree of lipophilicity, especially in a part mainly made up by hydrophobic amino acids like Tyr, Phe, Leu, or Val. The NADPH/NADP+-binding part of the catalytic site, on the other hand, is characterized by more hydrophilic amino acids and more polar properties overall. Due to the close vicinity of the co-substrate and substrate binding sites, the co-substrate NADPH/NADP+ may also contribute to the properties of the substrate cavity, introducing the possibility of polar interactions with a ligand bound in the folic acid binding site
additional information
-
enzyme structure modelling, residue Y163 is involved in catalysis
-
additional information
-
enzyme structure modelling, residue Y163 is involved in catalysis
-
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.
Nare, B.; Hardy, L.W.; Beverley, S.M.
The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major
J. Biol. Chem.
272
13883-13891
1997
Leishmania major, Leishmania tarentolae
brenda
Robello, C.; Navarro, P.; Castanys, S.; Gamarro, F.
A pteridine reductase gene ptr1 contiguous to a P-glycoprotein confers resistance to antifolates in Trypanosoma cruzi
Mol. Biochem. Parasitol.
90
525-535
1997
Trypanosoma cruzi, Trypanosoma cruzi Y
brenda
Nare, B.; Luba, J.; Hardy, L.W.; Beverley, S.
New approaches to Leishmania chemotherapy: pteridine reductase 1 (PTR1) as a target and modulator of antifolate sensitivity
Parasitology
114
101-110
1997
Leishmania major
-
brenda
Hardy, L.W.; Matthews, W.; Nare, B.; Beverley, S.M.
Biochemical and genetic tests for inhibitors of Leishmania pteridine pathways
Exp. Parasitol.
87
157-169
1997
Leishmania major
brenda
Leblanc, E.; Papadopoulou, B.; Bernatchez, C.; Ouellette, M.
Residues involved in co-factor and substrate binding of the short-chain dehydrogenase/reductase PTR1 producing methotrexate resistance in Leishmania
Eur. J. Biochem.
251
768-774
1998
Leishmania tarentolae
brenda
Bello, A.R.; Nare, B.; Freedman, D.; Hardy, L.; Beverly, S.M.
PTR1: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major
Proc. Natl. Acad. Sci. USA
91
11442-11446
1994
Leishmania major
brenda
Wang, J.; Leblanc, E.; Chang, C.F.; Papadopoulou, B.; Bray, T.; Witheley, J.M.; Lin, S.X.; Quellette, M.
Pterin and folate reduction by the Leishmania tarentolae H locus short-chain dehydrogenase/reductase PTR1
Arch. Biochem. Biophys.
342
197-202
1997
Leishmania tarentolae
brenda
Luba, J.; Nare, B.; Liang, P.H.; Anderson, K.S.; Beverley, S.M.; Hardy, L.W.
Leishmania major pteridine reductase 1 belongs to the short chain dehydrogenase family: stereochemical and kinetic evidence
Biochemistry
37
4093-4104
1998
Leishmania major
brenda
Zhao, H.; Bray, T.; Ouellette, M.; Zhao, M.; Ferre, R.A.; Matthews, D.; Whiteley, J.M.; Varughese, K.I.
Structure of pteridine reductase (PTR1) from Leishmania tarentolae
Acta Crystallogr. Sect. D
59
1539-1544
2003
Leishmania tarentolae (P42556), Leishmania tarentolae
brenda
McLuskey, K.; Gibellini, F.; Carvalho, P.; Avery, M.A.; Hunter, W.N.
Inhibition of Leishmania major pteridine reductase by 2,4,6-triaminoquinazoline: structure of the NADPH ternary complex
Acta Crystallogr. Sect. D
60
1780-1785
2004
Leishmania major (Q01782), Leishmania major
brenda
Kumar, P.; Kothari, H.; Singh, N.
Overexpression in Escherichia coli and purification of pteridine reductase (PTR1) from a clinical isolate of Leishmania donovani
Protein Expr. Purif.
38
228-236
2004
Leishmania donovani (Q6QDB5), Leishmania donovani
brenda
Schuettelkopf, A.W.; Hardy, L.W.; Beverley, S.M.; Hunter, W.N.
Structures of Leishmania major pteridine reductase complexes reveal the active site features important for ligand binding and to guide inhibitor design
J. Mol. Biol.
352
105-116
2005
Leishmania major
brenda
Dawson, A.; Gibellini, F.; Sienkiewicz, N.; Tulloch, L.B.; Fyfe, P.K.; McLuskey, K.; Fairlamb, A.H.; Hunter, W.N.
Structure and reactivity of Trypanosoma brucei pteridine reductase: inhibition by the archetypal antifolate methotrexate
Mol. Microbiol.
61
1457-1468
2006
Trypanosoma brucei
brenda
Kumar, P.; Sundar, S.; Singh, N.
Degradation of pteridine reductase 1 (PTR1) enzyme during growth phase in the protozoan parasite Leishmania donovani
Exp. Parasitol.
116
182-189
2007
Leishmania donovani (Q6QDB5), Leishmania donovani
brenda
Kumar, P.; Kumar, A.; Verma, S.S.; Dwivedi, N.; Singh, N.; Siddiqi, M.I.; Tripathi, R.P.; Dube, A.; Singh, N.
Leishmania donovani pteridine reductase 1: biochemical properties and structure-modeling studies
Exp. Parasitol.
120
73-79
2008
Leishmania donovani
brenda
Cavazzuti, A.; Paglietti, G.; Hunter, W.N.; Gamarro, F.; Piras, S.; Loriga, M.; Allecca, S.; Corona, P.; McLuskey, K.; Tulloch, L.; Gibellini, F.; Ferrari, S.; Costi, M.P.
Discovery of potent pteridine reductase inhibitors to guide antiparasite drug development
Proc. Natl. Acad. Sci. USA
105
1448-1453
2008
Trypanosoma cruzi, Leishmania major (Q01782), Leishmania major
brenda
Shanks, E.J.; Ong, H.B.; Robinson, D.A.; Thompson, S.; Sienkiewicz, N.; Fairlamb, A.H.; Frearson, J.A.
Development and validation of a cytochrome c-coupled assay for pteridine reductase 1 and dihydrofolate reductase
Anal. Biochem.
396
194-203
2010
Trypanosoma brucei (O76290), Trypanosoma brucei
brenda
Kaur, J.; Singh, B.K.; Tripathi, R.P.; Singh, P.; Singh, N.
Leishmania donovani: a glycosyl dihydropyridine analogue induces apoptosis like cell death via targeting pteridine reductase 1 in promastigotes
Exp. Parasitol.
123
258-264
2009
Leishmania donovani (Q6QDB5), Leishmania donovani
brenda
Mpamhanga, C.P.; Spinks, D.; Tulloch, L.B.; Shanks, E.J.; Robinson, D.A.; Collie, I.T.; Fairlamb, A.H.; Wyatt, P.G.; Frearson, J.A.; Hunter, W.N.; Gilbert, I.H.; Brenk, R.
One scaffold, three binding modes: novel and selective pteridine reductase 1 inhibitors derived from fragment hits discovered by virtual screening
J. Med. Chem.
52
4454-4465
2009
Trypanosoma brucei (O76290)
brenda
Singh, N.; Kaur, J.; Kumar, P.; Gupta, S.; Singh, N.; Ghosal, A.; Dutta, A.; Kumar, A.; Tripathi, R.; Siddiqi, M.I.; Mandal, C.; Dube, A.
An orally effective dihydropyrimidone (DHPM) analogue induces apoptosis-like cell death in clinical isolates of Leishmania donovani overexpressing pteridine reductase 1
Parasitol. Res.
105
1317-1325
2009
Leishmania donovani
brenda
Nare, B.; Garraway, L.A.; Vickers, T.J.; Beverley, S.M.
PTR1-dependent synthesis of tetrahydrobiopterin contributes to oxidant susceptibility in the trypanosomatid protozoan parasite Leishmania major
Curr. Genet.
55
287-299
2009
Leishmania major
brenda
Kaur, J.; Singh, N.; Singh, B.K.; Dube, A.; Tripathi, R.P.; Singh, P.; Singh, N.
Leishmania donovani: oral therapy with glycosyl 1,4-dihydropyridine analogue showing apoptosis like phenotypes targeting pteridine reductase 1 in intracellular amastigotes
Exp. Parasitol.
125
310-314
2010
Leishmania major
brenda
Kaur, J.; Sundar, S.; Singh, N.
Molecular docking, structure-activity relationship and biological evaluation of the anticancer drug monastrol as a pteridine reductase inhibitor in a clinical isolate of Leishmania donovani
J. Antimicrob. Chemother.
65
1742-1748
2010
Leishmania donovani
brenda
Tulloch, L.B.; Martini, V.P.; Iulek, J.; Huggan, J.K.; Lee, J.H.; Gibson, C.L.; Smith, T.K.; Suckling, C.J.; Hunter, W.N.
Structure-based design of pteridine reductase inhibitors targeting African sleeping sickness and the leishmaniases
J. Med. Chem.
53
221-229
2010
Leishmania major, Trypanosoma brucei (Q581W1), Trypanosoma brucei
brenda
Sienkiewicz, N.; Ong, H.B.; Fairlamb, A.H.
Trypanosoma brucei pteridine reductase 1 is essential for survival in vitro and for virulence in mice
Mol. Microbiol.
77
658-671
2010
Trypanosoma brucei
brenda
Barrack, K.L.; Tulloch, L.B.; Burke, L.A.; Fyfe, P.K.; Hunter, W.N.
Structure of recombinant Leishmania donovani pteridine reductase reveals a disordered active site
Acta Crystallogr. Sect. F
67
33-37
2011
Leishmania donovani (Q6QDB5), Leishmania donovani
brenda
Spinks, D.; Ong, H.B.; Mpamhanga, C.P.; Shanks, E.J.; Robinson, D.A.; Collie, I.T.; Read, K.D.; Frearson, J.A.; Wyatt, P.G.; Brenk, R.; Fairlamb, A.H.; Gilbert, I.H.
Design, synthesis and biological evaluation of novel inhibitors of Trypanosoma brucei pteridine reductase 1
ChemMedChem
6
302-308
2011
Trypanosoma brucei
brenda
Kazemi, B.; Tohidi, F.; Bandehpour, M.; Yarian, F.
Molecular cloning, expression and enzymatic assay of pteridine reductase 1 from Iranian lizard Leishmania
Iran. Biomed. J.
14
97-102
2010
Leishmania sp. (A2TEY0), Leishmania sp. BK-2007 (A2TEY0)
brenda
Ong, H.B.; Sienkiewicz, N.; Wyllie, S.; Fairlamb, A.H.
Dissecting the metabolic roles of pteridine reductase 1 in Trypanosoma brucei and Leishmania major
J. Biol. Chem.
286
10429-10438
2011
Leishmania major, Trypanosoma brucei
brenda
Sahi, S.; Tewatia, P.; Ghosal, S.
Leishmania donovani pteridine reductase 1: comparative protein modeling and protein-ligand interaction studies of the leishmanicidal constituents isolated from the fruits of Piper longum
J. Mol. Model.
18
5065-5073
2012
Leishmania donovani
brenda
Leite, F.H.A.; Froes, T.Q.; da Silva, S.G.; de Souza, E.I.M.; Vital-Fujii, D.G.; Trossini, G.H.G.; Pita, S.S.D.R.; Castilho, M.S.
An integrated approach towards the discovery of novel non-nucleoside Leishmania major pteridine reductase 1 inhibitors
Eur. J. Med. Chem.
132
322-332
2017
Leishmania major
brenda
de Souza Moreira, D.; Ferreira, R.F.; Murta, S.M.
Molecular characterization and functional analysis of pteridine reductase in wild-type and antimony-resistant Leishmania lines
Exp. Parasitol.
160
60-66
2016
Leishmania amazonensis (O09352), Leishmania amazonensis, Leishmania braziliensis (A4HCP1), Leishmania braziliensis, Leishmania guyanensis (A0A1E1IZ95), Leishmania guyanensis, Leishmania infantum (A4I067), Leishmania infantum
brenda
Khalaf, A.I.; Huggan, J.K.; Suckling, C.J.; Gibson, C.L.; Stewart, K.; Giordani, F.; Barrett, M.P.; Wong, P.E.; Barrack, K.L.; Hunter, W.N.
Structure-based design and synthesis of antiparasitic pyrrolopyrimidines targeting pteridine reductase 1
J. Med. Chem.
57
6479-6494
2014
Trypanosoma brucei
brenda
Di Pisa, F.; Landi, G.; Dello Iacono, L.; Pozzi, C.; Borsari, C.; Ferrari, S.; Santucci, M.; Santarem, N.; Cordeiro-Da-Silva, A.; Moraes, C.; Alcantara, L.; Fontana, V.; Freitas-Junior, L.; Gul, S.; Kuzikov, M.; Behrens, B.; Poehner, I.; Wade, R.; Costi,
Chroman-4-one derivatives targeting pteridine reductase 1 and showing anti-parasitic activity
Molecules
22
E426
2017
no activity in Homo sapiens, Trypanosoma brucei (O76290), Leishmania major (Q01782)
brenda
Landi, G.; Linciano, P.; Tassone, G.; Costi, M.P.; Mangani, S.; Pozzi, C.
High-resolution crystal structure of Trypanosoma brucei pteridine reductase 1 in complex with an innovative tricyclic-based inhibitor
Acta Crystallogr. Sect. D
76
558-564
2020
Trypanosoma brucei brucei (O76290)
brenda
Shamshad, H.; Hafiz, A.; Althagafi, I.I.; Saeed, M.; Mirza, A.Z.
Characterization of the Trypanosoma brucei pteridine reductase active-site using computational docking and virtual screening techniques
Curr. Comput. aided Drug Des.
16
583-598
2020
Trypanosoma brucei brucei (O76290), Leishmania major (Q01782), Leishmania major
brenda
Linciano, P.; Cullia, G.; Borsari, C.; Santucci, M.; Ferrari, S.; Witt, G.; Gul, S.; Kuzikov, M.; Ellinger, B.; Santarem, N.; Cordeiro da Silva, A.; Conti, P.; Bolognesi, M.L.; Roberti, M.; Prati, F.; Bartoccini, F.; Retini, M.; Piersanti, G.; Cavalli, A.; Goldoni, L.; Bertozzi, S.M.; Bertozzi, F.; , B.
Identification of a 2,4-diaminopyrimidine scaffold targeting Trypanosoma brucei pteridine reductase 1 from the LIBRA compound library screening campaign
Eur. J. Med. Chem.
189
112047
2020
Trypanosoma brucei brucei (O76290), Leishmania major (Q01782), Leishmania major
brenda
Phadke, S.; Somani, R.; Pathak, D.
New benzimidazole derivatives as inhibitors of Pteridine reductase 1 design, molecular docking study and ADMET prediction
J. Appl. Pharm. Sci.
10
30-39
2020
Leishmania major (Q01782)
-
brenda
Labine, M.; DePledge, L.; Feirer, N.; Greenwich, J.; Fuqua, C.; Allen, K.
Enzymatic and mutational analysis of the PruA pteridine reductase required for pterin-dependent control of biofilm formation in Agrobacterium tumefaciens
J. Bacteriol.
202
e00098-20
2020
Leishmania major (Q01782), Agrobacterium fabrum (Q7CZX3), Agrobacterium fabrum C58 (Q7CZX3), Agrobacterium fabrum ATCC 33970 (Q7CZX3)
brenda
Herrmann, F.C.; Sivakumar, N.; Jose, J.; Costi, M.P.; Pozzi, C.; Schmidt, T.J.
In silico identification and in vitro evaluation of natural inhibitors of Leishmania major pteridine reductase I
Molecules
22
2166
2017
Leishmania major (Q01782), Leishmania major
brenda
Kimuda, M.P.; Laming, D.; Hoppe, H.C.; Tastan Bishop, Oe.
Identification of novel potential inhibitors of pteridine reductase 1 in Trypanosoma brucei via computational structure-based approaches and in vitro inhibition assays
Molecules
24
142
2019
Trypanosoma cruzi (O44029), Trypanosoma brucei brucei (O76290)
brenda
Herrera-Acevedo, C.; Flores-Gaspar, A.; Scotti, L.; Mendonca-Junior, F.J.B.; Scotti, M.T.; Coy-Barrera, E.
Identification of kaurane-type diterpenes as inhibitors of Leishmania pteridine reductase I
Molecules
26
0000
2021
Leishmania panamensis (A0A088SA10), Leishmania panamensis, Leishmania braziliensis (A4HCP1), Leishmania amazonensis (O09352), Leishmania major (Q01782), Leishmania major
brenda
Tassone, G.; Landi, G.; Linciano, P.; Francesconi, V.; Tonelli, M.; Tagliazucchi, L.; Costi, M.P.; Mangani, S.; Pozzi, C.
Evidence of pyrimethamine and cycloguanil analogues as dual inhibitors of Trypanosoma brucei pteridine reductase and dihydrofolate reductase
Pharmaceuticals
14
636
2021
Trypanosoma brucei brucei (O76290)
brenda
Bhattacharya, A.; Leprohon, P.; Ouellette, M.
Combined gene deletion of dihydrofolate reductase-thymidylate synthase and pteridine reductase in Leishmania infantum
PLoS Negl. Trop. Dis.
15
e0009377
2021
Leishmania infantum (A4I067), Leishmania infantum, Leishmania infantum MHOM/MA/67/ITMAP-263 (A4I067)
brenda