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Literature summary for 1.5.1.6 extracted from
- Domain structure and function of 10-formyltetrahydrofolate dehydrogenase (1994), J. Biol. Chem., 269, 24728-24735.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| NADPH | activates | Oryctolagus cuniculus |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| chymotrypsin | cleavage between the two domains, inactivates 10-formyltetrahydrofolate dehydrogenase but not hydrolase and aldehyde dehydrogenase activity | Oryctolagus cuniculus | |
| Subtilisin | cleavage between the two domains, inactivates 10-formyltetrahydrofolate dehydrogenase but not hydrolase and aldehyde dehydrogenase activity | Oryctolagus cuniculus | |
| tetrahydrofolate | - |
Oryctolagus cuniculus | |
| Trypsin | cleavage between the two domains, inactivates 10-formyltetrahydrofolate dehydrogenase but not hydrolase and aldehyde dehydrogenase activity | Oryctolagus cuniculus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.001 | - |
NADP+ | - |
Oryctolagus cuniculus | |
| 0.013 | - |
10-formyltetrahydrofolate | - |
Oryctolagus cuniculus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 99000 | - |
4 * 99000, SDS-PAGE | Oryctolagus cuniculus |
| 440000 | - |
gel filtration | Oryctolagus cuniculus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 10-formyltetrahydrofolate + NADP+ + H2O | Oryctolagus cuniculus | regulation of the ratio of 10-formyltetrahydrofolate to tetrahydrofolate in the cell in response to yet unknown aldehyde and thiol metabolites | tetrahydrofolate + CO2 + NADPH + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Oryctolagus cuniculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Oryctolagus cuniculus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Oryctolagus cuniculus |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -20°C, 20% glycerol, several months, stable | Oryctolagus cuniculus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 10-formyltetrahydrofolate + NADP+ + H2O | structure of enzyme domains and of catalytic centers | Oryctolagus cuniculus | tetrahydrofolate + CO2 + NADPH + H+ | high affinity for tetrahydrofolate | ? | |
| 10-formyltetrahydrofolate + NADP+ + H2O | enzyme requires Cys-707 to form a thiohemiacetal with the formyl group of 10-formyltetrahydrofolate | Oryctolagus cuniculus | tetrahydrofolate + CO2 + NADPH + H+ | high affinity for tetrahydrofolate | ? | |
| 10-formyltetrahydrofolate + NADP+ + H2O | enzyme binds one molecule of tetrahydrofolate and two molecules of NADP+ per tetramer, tetrahydrofolate and NADP+ bind to separate domains, higher affinity for NADP+ at lower enzyme concentrations | Oryctolagus cuniculus | tetrahydrofolate + CO2 + NADPH + H+ | high affinity for tetrahydrofolate | ? | |
| 10-formyltetrahydrofolate + NADP+ + H2O | regulation of the ratio of 10-formyltetrahydrofolate to tetrahydrofolate in the cell in response to yet unknown aldehyde and thiol metabolites | Oryctolagus cuniculus | tetrahydrofolate + CO2 + NADPH + H+ | - |
? | |
| additional information | enzyme exhibit additional to 10-formyltetrahydrofolate dehydrogenase/hydrolase activities NADP+-dependent aldehyde dehydrogenase activity with propanal as preferred substrate | Oryctolagus cuniculus | ? | - |
? | |
| additional information | enzyme consists of two independent folded domains connected by a linker sequence: a 32 kDa N-terminal domain with 10-formyltetrahydrofolate binding site shows hydrolase activity and a 63 kDa C-terminal domain with NADP+ binding site and Cys-707 shows aldehyde dehydrogenase activity, native structure of enzyme is necessary for 10-formyltetrahydrofolate dehydrogenase activity | Oryctolagus cuniculus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | 4 * 99000, SDS-PAGE | Oryctolagus cuniculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Oryctolagus cuniculus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.967 | - |
10-formyltetrahydrofolate | - |
Oryctolagus cuniculus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
broad pH-maximum at pH 8.0 | Oryctolagus cuniculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 10-formyltetrahydrofolate | 10-formyltetrahydrofolate | Oryctolagus cuniculus | |
| NADP+ | NADP+-dependent | Oryctolagus cuniculus | |
| tetrahydrofolate | - |
Oryctolagus cuniculus | |
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