1.5.1.33: pteridine reductase
This is an abbreviated version!
For detailed information about pteridine reductase, go to the full flat file.
Word Map on EC 1.5.1.33
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1.5.1.33
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leishmania
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dihydrofolate
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trypanosoma
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antileishmanial
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antifolate
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promastigotes
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leishmaniasis
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trypanosomatids
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pterins
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donovani
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amastigotes
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trypanosomiasis
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dhfr-t
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trypanothione
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reductase-thymidylate
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tarentolae
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dihydrobiopterin
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glucantime
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medicine
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drug development
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pharmacology
- 1.5.1.33
- leishmania
- dihydrofolate
- trypanosoma
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antileishmanial
- antifolate
- promastigotes
- leishmaniasis
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trypanosomatids
- pterins
- donovani
- amastigotes
- trypanosomiasis
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dhfr-t
- trypanothione
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reductase-thymidylate
- tarentolae
- dihydrobiopterin
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glucantime
- medicine
- drug development
- pharmacology
Reaction
Synonyms
Atu1130, EC 1.1.1.253, H region methotrexate resistance protein, LaPTR1, LbPTR1, LdPTR1, LmPTR1, LpPTR1, More, NADPH-dependent short-chain dehydrogenase/reductase pteridine reductase, NADPH-dihydropteridine reductase, PruA, pteridine reductase, pteridine reductase 1, pteridine reductase I, PTR1, reductase, dihydropteridine (reduced nicotinamide adenine dinucleotide phosphate), Tb-PR, TbPTR1, tcptr1
ECTree
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Substrates Products
Substrates Products on EC 1.5.1.33 - pteridine reductase
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REACTION DIAGRAM
dihydrobiopterin + tetrahydrobiopterin + 3 NADP+
essential enzyme of pterin and folate metabolism
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2 biopterin + 3 NADPH + 3 H+
dihydrobiopterin + tetrahydrobiopterin + 3 NADP+
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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)
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6-biopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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5,6,7,8-tetrahydrobiopterin + NADP+
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
low activity
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
best substrate
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7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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5,6,7,8-tetrahydrofolate + NADP+
low activity
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7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
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7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
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5,6,7,8-tetrahydromonapterin + NADP+
cf. EC 1.5.1.50, moderate activity
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7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
cf. EC 1.5.1.50, moderate activity
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7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
cf. EC 1.5.1.50, moderate activity
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5,6,7,8-tetrahydroneopterin + NADP+
stereoisomer of biopterin, moderate activity
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7,8-dihydroneopterin + NADPH + H+
5,6,7,8-tetrahydroneopterin + NADP+
stereoisomer of biopterin, moderate activity
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7,8-dihydroneopterin + NADPH + H+
5,6,7,8-tetrahydroneopterin + NADP+
stereoisomer of biopterin, moderate activity
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5,6,7,8-tetrahydrobiopterin + 2 NADP+
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biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
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biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
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biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
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biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
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biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
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biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
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biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
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biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
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biopterin + 2 NADPH + 2 H+
5,6,7,8-tetrahydrobiopterin + 2 NADP+
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substrate binding structure
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Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
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Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
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activity with NADH is less than 5% of the activity with NADPH
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Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
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Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
2-step reaction via intermediate 7,8-dihydrobiopterin
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Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
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no activity with NADH and NADP+
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Biopterin + NADPH
5,6,7,8-Tetrahydrobiopterin + NADP+
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no activity with NADH and NADP+
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biopterin + NADPH + H+
7,8-dihydrobiopterin + NADP+
best substrate
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biopterin + NADPH + H+
7,8-dihydrobiopterin + NADP+
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dihydrobiopterin + NADPH
5,6,7,8-tetrahydrobiopterin + NADP+
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r
dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
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5,6,7,8-Tetrahydrofolate + NADP+
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7,8-dihydrofolate + NADP+
high activity, see also EC 1.5.1.3
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folate + NADPH + H+
7,8-dihydrofolate + NADP+
reaction of EC 1.5.1.3
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7,8-dihydrofolate + tetrahydrofolate + NADP+
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folate + NADPH + H+
7,8-dihydrofolate + tetrahydrofolate + NADP+
essential enzyme of pterin and folate metabolism
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tetrahydrobiopterin + NADP+
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quinonoid dihydrobiopterin + NADPH + H+
tetrahydrobiopterin + NADP+
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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
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additional information
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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
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additional information
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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
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additional information
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enzyme is associated with folate metabolism, responsible for salvage of pterins and reduction of folates
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additional information
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enzyme is associated with folate metabolism, responsible for salvage of pterins and reduction of folates
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additional information
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NADPH binds first, the enzyme-NADPH complex binds the substrate
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additional information
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NADPH binds first, the enzyme-NADPH complex binds the substrate
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additional information
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no activity with quinoid dihydrobiopterin
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additional information
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primary enzyme mediating pteridine salvage
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additional information
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the enzyme mediates the synthesis of tetrahydropteridines
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additional information
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essential for the salvage of pterins
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additional information
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enzyme PTR1 synthesizes the formation of tetrahydrobiopterin from biopterin via dihydrobiopterin or from the quinoide form dihydrobiopterin, pathway overview
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additional information
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enzyme PTR1 synthesizes the formation of tetrahydrobiopterin from biopterin via dihydrobiopterin or from the quinoide form dihydrobiopterin, pathway overview
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additional information
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7,8-dihydro-L-biopterin and pyrimethamine (PMA) interact with enzyme residues S112, Y194, L226, and S227, molecular dynamics and docking study, overview
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additional information
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7,8-dihydro-L-biopterin and pyrimethamine (PMA) interact with enzyme residues S112, Y194, L226, and S227, molecular dynamics and docking study, overview
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additional information
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the enzyme mediates the synthesis of tetrahydropteridines
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additional information
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enzyme is used by the organism to bypass antifolate inhibition, catalytic pathway
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additional information
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enzyme is used by the organism to bypass antifolate inhibition, catalytic pathway
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additional information
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enzyme PTR1 synthesizes the formation of tetrahydrobiopterin from biopterin via dihydrobiopterin or from the quinoide form dihydrobiopterin, pathway overview
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additional information
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the enzyme is involved in the resistance to the methotrexate, aminopterin and trimethoprim antifolates
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additional information
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the enzyme is involved in the resistance to the methotrexate, aminopterin and trimethoprim antifolates
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