General Stability | Organism |
---|---|
extremely sensitive to proteolysis | Sus scrofa |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
dihydrofolate | - |
Sus scrofa | |
dihydropteroylhexaglutamate | - |
Sus scrofa | |
dihydropteroylpolyglutamate | most potent inhibitor is dihydropteroylhexaglutamate | Sus scrofa | |
S-adenosylmethionine | inhibition partially reversed by S-adenosylhomocysteine | Sus scrofa |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.016 | - |
NADPH | 5,10-methylenetetrahydrofolate reductase reaction, pH 7.2 | Sus scrofa | |
0.019 | - |
5,10-methylenetetrahydrofolate | methylenetetrahydrofolate reductase reaction, pH 6.7 | Sus scrofa | |
0.088 | - |
5,10-methylenetetrahydrofolate | methylenetetrahydrofolate reductase reaction, pH 7.2 | Sus scrofa |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
77300 | - |
SDS-PAGE | Sus scrofa |
136000 | - |
scanning transmission electron microscopy | Sus scrofa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
5,10-methylenetetrahydrofolate + NADPH | Sus scrofa | initial enzyme in pathway leading to synthesis of S-adenosylmethionine | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
Purification (Comment) | Organism |
---|---|
homogeneity | Sus scrofa |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+ | mechanism | Sus scrofa |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Sus scrofa | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
different assay methods | Sus scrofa |
19.4 | - |
- |
Sus scrofa |
Storage Stability | Organism |
---|---|
-70°C, 10% glycerol, several months | Sus scrofa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-pyrroline-5-carboxylate + NADH + H+ | - |
Sus scrofa | L-proline + NAD+ | - |
r | |
5,10-methylenetetrahydrofolate + NADPH | ping pong kinetics | Sus scrofa | 5-methyltetrahydrofolate + NADP+ | - |
? | |
5,10-methylenetetrahydrofolate + NADPH | enzyme also catalyzes the NADPH-linked reduction of quinoid dihydrofolate and dihydropterin derivates | Sus scrofa | 5-methyltetrahydrofolate + NADP+ | - |
? | |
5,10-methylenetetrahydrofolate + NADPH | initial enzyme in pathway leading to synthesis of S-adenosylmethionine | Sus scrofa | ? | - |
? | |
5-methyltetrahydrofolate + oxidized menadione | ping pong kinetics | Sus scrofa | 5,10-methylenetetrahydrofolate + reduced menadione | - |
? | |
NADPH + H+ + menadione | ping pong kinetics | Sus scrofa | NADP+ + menadiol | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | dimer or trimer, 2 or 3 * 77300, SDS-PAGE | Sus scrofa |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
160 | - |
NADH | - |
Sus scrofa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | flavoprotein | Sus scrofa | |
FAD | each subunit contains noncovalently bound FAD | Sus scrofa |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000013 | - |
dihydropteroylhexaglutamate | - |
Sus scrofa |