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Literature summary for 1.5.1.54 extracted from
- Purification and properties of a NADH-dependent 5,10-methylenetetrahydrofolate reductase from Peptostreptococcus productus (1990), Eur. J. Biochem., 192, 411-417 .
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.01 | - |
NADH | pH 5.5, 37°C | Blautia producta |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | associated to membrane | Blautia producta | 16020 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 250000 | - |
gel filtration | Blautia producta |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydrofolate + NADH + H+ | Blautia producta | - |
5-methyltetrahydrofolate + NAD+ | - |
? | |
| 5,10-methylenetetrahydrofolate + NADH + H+ | Blautia producta Marburg | - |
5-methyltetrahydrofolate + NAD+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Blautia producta | - |
- |
- |
| Blautia producta Marburg | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Blautia producta |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 380 | - |
pH 5.5, 37°C | Blautia producta |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5,10-methylenetetrahydrofolate + NADH + H+ | - |
Blautia producta | 5-methyltetrahydrofolate + NAD+ | - |
? | |
| 5,10-methylenetetrahydrofolate + NADH + H+ | - |
Blautia producta Marburg | 5-methyltetrahydrofolate + NAD+ | - |
? | |
| 5,10-methylenetetrahydrofolate + reduced methylene blue | - |
Blautia producta | 5-methyltetrahydrofolate + methylene blue | - |
r | |
| 5,10-methylenetetrahydrofolate + reduced methylene blue | - |
Blautia producta Marburg | 5-methyltetrahydrofolate + methylene blue | - |
r | |
| 5-methyltetrahydrofolate + methylene blue | - |
Blautia producta | 5,10-methylenetetrahydrofolate + reduced methylene blue | - |
r | |
| 5-methyltetrahydrofolate + methylene blue | - |
Blautia producta Marburg | 5,10-methylenetetrahydrofolate + reduced methylene blue | - |
r | |
| additional information | the enzyme catalyzes the methylenetetrahydrofolate reduction with methylene blue as an artificial electron donor. The oxidation of methyltetrahydrofolate is mediated with methylene blue as the electron acceptor. Neither NAD+ nor viologen dyes can replace methylene blue in this reaction | Blautia producta | ? | - |
- |
|
| additional information | the enzyme catalyzes the methylenetetrahydrofolate reduction with methylene blue as an artificial electron donor. The oxidation of methyltetrahydrofolate is mediated with methylene blue as the electron acceptor. Neither NAD+ nor viologen dyes can replace methylene blue in this reaction | Blautia producta Marburg | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| octamer | 8 * 32000, SDS-PAGE | Blautia producta |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | 4 FAD/mol octamer | Blautia producta | |
| additional information | no cosubstrates: NADPH, FAD(H2) | Blautia producta | |
| NADH | - |
Blautia producta | |
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