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Literature summary for 1.16.1.8 extracted from
- Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation (2001), J. Biol. Chem., 276, 35558-35563.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00264 | - |
NADPH | - |
Homo sapiens |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | - |
Homo sapiens | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 77000 | - |
gel filtration | Homo sapiens |
| 78000 | - |
1 * 78000, SDS-PAGE | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Homo sapiens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1.56 | - |
- |
Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| [methionine synthase]-cob(II)alamin + NADH + S-adenosyl-L-methionine | - |
Homo sapiens | [methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + NAD+ | - |
? | |
| [Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl-L-methionine | - |
Homo sapiens | [Methionine synthase]methylcob(I)alamin + S-adenosylhomocysteine + NADP+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 78000, SDS-PAGE | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Methionine synthase reductase | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | dual flavoprotein with an equimolar concentration of FAD, 0.9 mol per mol of enzyme, and FMN, 1.1 mol per mol of enzyme | Homo sapiens | |
| FMN | dual flavoprotein with an equimolar concentration of FAD, 0.9 mol per mol of enzyme, and FMN, 1.1 mol per mol of enzyme | Homo sapiens | |
| NADH | can replace NADPH but only at significantly higher and nonphysiological concentrations | Homo sapiens | |
| NADPH | preferred electron donor | Homo sapiens | |
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Release 2023.1 (January 2023)
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