Application | Comment | Organism |
---|---|---|
drug development | the enzyme is considered a promising target for anti-leishmanial drug development and several inhibitors that share the substrate scaffold | Leishmania major |
Cloned (Comment) | Organism |
---|---|
gene PTR1, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Leishmania major |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(Z)-5-(2,4-dichlorobenzylidene)-thiazolidine-2,4-dione | - |
Leishmania major | |
(Z)-5-(2-bromo-5-methoxybenzylidene)-thiazolidine-2,4-dione | - |
Leishmania major | |
(Z)-5-(2-bromo-6-fluorobenzylidene)-thiazolidine-2,4-dione | - |
Leishmania major | |
(Z)-5-(2-hydroxy-3-bromo-5-chlorobenzylidene)-thiazolidine-2,4-dione | a noncompetitive inhibitor that binds in the same site as the cofactor | Leishmania major | |
(Z)-5-(2-hydroxy-5-chlorobenzylidene)-thiazolidine-2,4-dione | - |
Leishmania major | |
5-(3,4-dichlorobenzylidene)-thiazolidine-2,4-dione | - |
Leishmania major | |
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 | Leishmania major |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics, thermal shift assay | Leishmania major |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
biopterin + 2 NADPH + 2 H+ | Leishmania major | - |
5,6,7,8-tetrahydrobiopterin + 2 NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leishmania major | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
5,6,7,8-tetrahydrobiopterin + 2 NADP+ = biopterin + 2 NADPH + 2 H+ | the enzyme exhhibits a ping-pong mechanism | Leishmania major |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
biopterin + 2 NADPH + 2 H+ | - |
Leishmania major | 5,6,7,8-tetrahydrobiopterin + 2 NADP+ | - |
? | |
additional information | thermal shift enzyme assay optimization | Leishmania major | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
pteridine reductase 1 | - |
Leishmania major |
PTR1 | - |
Leishmania major |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Leishmania major |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
midpoint temperatures of the LmPTR1-unfolding transition (Tm) at different pHs, DMSO concentrations, and inhibitor concentrations, thermal shift enzyme assay optimization, overview | Leishmania major |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.7 | - |
assay at | Leishmania major |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4.5 | 7.5 | enzyme LmPTR1 is stable either in pH 4.5 or pH 7.5, since Tm values does not vary significantly between these conditions | Leishmania major |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Leishmania major |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | inhibition kinetics, thermal shift assay | Leishmania major |