EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.3 | Cl- | - |
Homo sapiens | |
1.5.1.3 | Cl- | a few bacterial and vertebrate enzymes are activated at concentrations of 0.3-0.5 M | Bacteria | |
1.5.1.3 | Cl- | a few bacterial and vertebrate enzymes are activated at concentrations of 0.3-0.5 M | vertebrata | |
1.5.1.3 | Urea | - |
Homo sapiens | |
1.5.1.3 | Urea | - |
Lacticaseibacillus casei | |
1.5.1.3 | Urea | increase in Km and kcat values for 7,8-dihydrofolate and NADPH | Gallus gallus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.5.1.3 | binding to trimethoprim, structure analysis | Escherichia coli |
1.5.1.3 | comparison of the backbone conformation in crystal structures, detection of mutational insertions | Bacteria |
1.5.1.3 | comparison of the backbone conformation in crystal structures, detection of mutational insertions | vertebrata |
1.5.1.3 | no crystallographic data available, but model-based structure analysis | Homo sapiens |
1.5.1.3 | structure of ternary complex with NADPH and methotrexate | Escherichia coli |
1.5.1.3 | structure of ternary complex with NADPH and methotrexate | Lacticaseibacillus casei |
1.5.1.3 | structure of ternary complex with NADPH and phenyltriazine | Lacticaseibacillus casei |
1.5.1.3 | structure of ternary complex with NADPH and trimethoprim, model development | Gallus gallus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.5.1.3 | additional information | - |
Mus musculus |
1.5.1.3 | additional information | overview about spontaneously occuring mutants and possible mutagenesis studies | Bacteria |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.3 | 2,4-diamino-5-methyl-butylpyrido[2,3-d]pyrimidine | - |
Bacteria | |
1.5.1.3 | 2,4-Dimamino-6-butylpyrido[2,3-d]pyrimidine | - |
Bacteria | |
1.5.1.3 | methotrexate | - |
Bacteria | |
1.5.1.3 | methotrexate | - |
Escherichia coli | |
1.5.1.3 | methotrexate | - |
Gallus gallus | |
1.5.1.3 | methotrexate | - |
Homo sapiens | |
1.5.1.3 | methotrexate | - |
Lacticaseibacillus casei | |
1.5.1.3 | methotrexate | - |
Mus musculus | |
1.5.1.3 | additional information | overview; stereochemistry of inhibitor binding | Bacteria | |
1.5.1.3 | additional information | overview; stereochemistry of inhibitor binding | Escherichia coli | |
1.5.1.3 | additional information | overview; stereochemistry of inhibitor binding | Gallus gallus | |
1.5.1.3 | additional information | overview; stereochemistry of inhibitor binding | Lacticaseibacillus casei | |
1.5.1.3 | additional information | overview | Mus musculus | |
1.5.1.3 | additional information | overview | Pigeon | |
1.5.1.3 | additional information | stereochemistry of inhibitor binding | protozoa | |
1.5.1.3 | additional information | stereochemistry of inhibitor binding | vertebrata | |
1.5.1.3 | pyrimethamine | i.e. 2,4-diamino-5-p-chlorophenyl-6-ethylpyridine | Bacteria | |
1.5.1.3 | pyrimethamine | - |
Gallus gallus | |
1.5.1.3 | pyrimethamine | - |
Homo sapiens | |
1.5.1.3 | pyrimethamine | - |
Mus musculus | |
1.5.1.3 | trimethoprim | - |
Bacteria | |
1.5.1.3 | trimethoprim | - |
Escherichia coli | |
1.5.1.3 | trimethoprim | - |
Gallus gallus | |
1.5.1.3 | trimethoprim | - |
Homo sapiens | |
1.5.1.3 | trimethoprim | - |
Lacticaseibacillus casei | |
1.5.1.3 | trimethoprim | - |
Mus musculus | |
1.5.1.3 | trimethoprim | - |
vertebrata |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.1.3 | 0.00047 | - |
7,8-dihydrofolate | - |
Escherichia coli | |
1.5.1.3 | 0.0025 | 0.0032 | NADPH | - |
Escherichia coli | |
1.5.1.3 | 0.268 | - |
NADH | - |
Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.5.1.3 | 35000 | - |
bacterial isozyme type II, R factor encoded | Bacteria |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.3 | 7,8-dihydrofolate + NADPH | Homo sapiens | - |
5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | Gallus gallus | maintainance of adequate levels of fully reduced folate in metabolism of proliferating cells | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | Bacteria | maintainance of adequate levels of fully reduced folate in metabolism of proliferating cells | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | Bacteria | directly correlated with thymidylate synthesis | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.3 | Bacteria | - |
overview | - |
1.5.1.3 | Escherichia coli | - |
- |
- |
1.5.1.3 | Gallus gallus | - |
- |
- |
1.5.1.3 | Homo sapiens | - |
methotrexate-resistant WIL-2 lymphoblastoid cells | - |
1.5.1.3 | Klebsiella aerogenes | - |
R-plasmid encoded, trimethoprim-resistant | - |
1.5.1.3 | Lacticaseibacillus casei | - |
- |
- |
1.5.1.3 | Mus musculus | - |
L1210 lymphoma cells, amethopterin-resistant | - |
1.5.1.3 | Pigeon | - |
- |
- |
1.5.1.3 | protozoa | - |
- |
- |
1.5.1.3 | vertebrata | - |
overview | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ | rapid equilibrium random mechanism | Bacteria | |
1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ | catalytic mechanism | Bacteria | |
1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ | catalytic mechanism | Escherichia coli | |
1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ | catalytic mechanism | Lacticaseibacillus casei | |
1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ | catalytic mechanism | vertebrata | |
1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ | catalytic mechanism | protozoa | |
1.5.1.3 | 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ | substrate and cofactor binding mechanism | Bacteria |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.3 | 7,8-dihydrofolate + NADH + H+ | - |
Escherichia coli | 5,6,7,8-tetrahydrofolate + NAD+ | - |
r | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | - |
Gallus gallus | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | - |
Mus musculus | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | - |
Homo sapiens | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | - |
Pigeon | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | - |
vertebrata | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | - |
protozoa | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | equilibrium strongly favors tetrahydrofolate production | Bacteria | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | equilibrium strongly favors tetrahydrofolate production | Bacteria | 5,6,7,8-tetrahydrofolate + NADP+ | - |
r | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | equilibrium strongly favors tetrahydrofolate production | Escherichia coli | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | equilibrium strongly favors tetrahydrofolate production | Escherichia coli | 5,6,7,8-tetrahydrofolate + NADP+ | - |
r | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | equilibrium strongly favors tetrahydrofolate production | Lacticaseibacillus casei | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | equilibrium strongly favors tetrahydrofolate production | Lacticaseibacillus casei | 5,6,7,8-tetrahydrofolate + NADP+ | - |
r | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | maintainance of adequate levels of fully reduced folate in metabolism of proliferating cells | Gallus gallus | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | maintainance of adequate levels of fully reduced folate in metabolism of proliferating cells | Bacteria | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
1.5.1.3 | 7,8-dihydrofolate + NADPH | directly correlated with thymidylate synthesis | Bacteria | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.5.1.3 | dimer | - |
Escherichia coli |
1.5.1.3 | dimer | isozymes type I | Bacteria |
1.5.1.3 | monomer | - |
Gallus gallus |
1.5.1.3 | monomer | - |
Mus musculus |
1.5.1.3 | monomer | - |
Escherichia coli |
1.5.1.3 | monomer | - |
Lacticaseibacillus casei |
1.5.1.3 | monomer | isozymes type III | Bacteria |
1.5.1.3 | More | overview | Bacteria |
1.5.1.3 | More | overview | protozoa |
1.5.1.3 | tetramer | 4 * 8500-9000, R-plasmid-coded type II reductase | Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.1.3 | 16.5 | - |
7,8-dihydrofolate | - |
Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.5.1.3 | 4.5 | - |
folic acid reduction | Bacteria |
1.5.1.3 | 4.5 | - |
folic acid reduction | Escherichia coli |
1.5.1.3 | 7 | - |
- |
Escherichia coli |
1.5.1.3 | 7 | - |
7,8-dihydrofolate reduction | Bacteria |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.3 | NADPH | - |
Bacteria | |
1.5.1.3 | NADPH | - |
Mus musculus | |
1.5.1.3 | NADPH | - |
Homo sapiens | |
1.5.1.3 | NADPH | - |
Pigeon | |
1.5.1.3 | NADPH | - |
vertebrata | |
1.5.1.3 | NADPH | cofactor-enzyme interaction study from x-ray structure, structural and topological comparison with dehydrogenases | Gallus gallus | |
1.5.1.3 | NADPH | cofactor-enzyme interaction study from x-ray structure, structural and topological comparison with dehydrogenases | Escherichia coli | |
1.5.1.3 | NADPH | cofactor-enzyme interaction study from x-ray structure, structural and topological comparison with dehydrogenases | Lacticaseibacillus casei |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.1.3 | additional information | - |
additional information | - |
Gallus gallus | |
1.5.1.3 | additional information | - |
additional information | - |
Mus musculus | |
1.5.1.3 | additional information | - |
additional information | - |
Escherichia coli | |
1.5.1.3 | additional information | - |
additional information | - |
Homo sapiens | |
1.5.1.3 | additional information | - |
additional information | - |
Lacticaseibacillus casei | |
1.5.1.3 | additional information | - |
additional information | overview, effect of methotrexate and trimethoprim | Bacteria | |
1.5.1.3 | additional information | - |
additional information | overview, effect of methotrexate and trimethoprim | vertebrata | |
1.5.1.3 | additional information | - |
additional information | overview, effect of methotrexate and trimethoprim | protozoa | |
1.5.1.3 | 0.000004 | - |
trimethoprim | bacterial chromosomal encoded isozyme type I | Bacteria | |
1.5.1.3 | 0.000019 | - |
trimethoprim | bacterial chromosomal encoded isozyme type III | Bacteria | |
1.5.1.3 | 0.00009 | - |
methotrexate | bacterial, R factor encoded isozyme type II | Bacteria | |
1.5.1.3 | 0.01 | - |
trimethoprim | bacterial, R factor encoded isozymes type I | Bacteria |