EC Number | Application | Comment | Organism |
---|---|---|---|
1.5.1.20 | medicine | C677T mution of MTHRF gene is the most frequent genetic cause of mild hyperhomocysteinemia, a risk factor for cardiovascular disease | Homo sapiens |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.1.20 | expression of recombinant human MTHFR at high levels in Sf9 cells from Spodoptera frugiperda by using a baculovirus expression system | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.5.1.20 | A177V | enzyme with decreased affinity for its FAD cofactor | Escherichia coli |
1.5.1.20 | A222V | most frequent genetic cause of mild hyperhomocysteinemia, enzyme with enhanced propensity to dissociate into monomers and to lose its FAD cofactor on dilution, increased thermolability of enzyme activity | Homo sapiens |
1.5.1.20 | E429A | A1298C mutation of the MTHRF gene, enzyme with indistinguishable properties from the wild-type | Homo sapiens |
1.5.1.20 | additional information | C677T mutation in MTHFR gene is a polymorphism which leads to the substitution of Ala-222 by valine | Homo sapiens |
1.5.1.20 | additional information | A1298C mutation of the MTHFR gene, which leads to the substitution of Glu-429 by alanine | Homo sapiens |
EC Number | General Stability | Organism |
---|---|---|
1.5.1.20 | methyltetrahydrofolate and S-adenosylmethionine protects enzyme from the loss of FAD after dilution | Escherichia coli |
1.5.1.20 | methyltetrahydrofolate and S-adenosylmethionine protects enzyme from the loss of FAD after dilution | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.20 | S-adenosylmethionine | strong, reversible allosteric inhibition, prevented by S-adenosylhomocysteine | Homo sapiens |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.5.1.20 | 33000 | - |
4 * 33000 | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.20 | 5,10-methylenetetrahydrofolate + NADPH | Homo sapiens | physiological NADPH-CH2-H4folate oxidoreductase activity | 5-methyltetrahydrofolate + NADP+ | 5-methyltetrahydrofolate is the major methyl donor for the conversion of homocysteine to methionine | ? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.20 | Escherichia coli | - |
- |
- |
1.5.1.20 | Homo sapiens | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.5.1.20 | 62fold purification of recombinant enzyme, expressed in Sf9 cells from Spodoptera frugiperda | Homo sapiens |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.5.1.20 | 12.4 | - |
recombinant enzyme | Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.20 | 5,10-methylenetetrahydrofolate + NADPH | physiological NADPH-CH2-H4folate oxidoreductase activity | Homo sapiens | 5-methyltetrahydrofolate + NADP+ | 5-methyltetrahydrofolate is the major methyl donor for the conversion of homocysteine to methionine | ? | |
1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced acceptor | forward reaction: NADPH as reduced acceptor | Escherichia coli | 5-methyltetrahydrofolate + oxidized acceptor | - |
? | |
1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced acceptor | forward reaction: NADPH as reduced acceptor | Homo sapiens | 5-methyltetrahydrofolate + oxidized acceptor | - |
? | |
1.5.1.20 | 5,10-methylenetetrahydrofolate + reduced acceptor | forward reaction: NADH as reduced acceptor | Escherichia coli | 5-methyltetrahydrofolate + oxidized acceptor | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.5.1.20 | dimer | - |
Homo sapiens |
1.5.1.20 | homotetramer | 4 * 33000 | Escherichia coli |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.1.20 | additional information | - |
thermolability is enhanced when the FAD cofactor dissociates form enzyme | Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.1.20 | FAD | flavoprotein with FAD as cofactor | Escherichia coli | |
1.5.1.20 | FAD | flavoprotein with FAD as cofactor | Homo sapiens | |
1.5.1.20 | FAD | FAD is essential for electron transfer between NADH and methylenetetrahydrofolate | Escherichia coli | |
1.5.1.20 | NADH | - |
Escherichia coli | |
1.5.1.20 | NADPH | - |
Escherichia coli | |
1.5.1.20 | NADPH | - |
Homo sapiens |