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Literature summary extracted from
- Escherichia coli glyoxalate carboligase (1976), J. Biol. Chem., 251, 329-333.
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.1.1.47 | 68000 | - |
2 * 68000, SDS-PAGE | Escherichia coli |
| 4.1.1.47 | 145000 | - |
gel filtration | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.47 | Escherichia coli | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.1.47 | - |
Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.1.47 | Glyoxylate | - |
Escherichia coli | Tartronate semialdehyde + CO2 | - |
? |  |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.1.1.47 | dimer | 2 * 68000, SDS-PAGE | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.1.47 | 1,5-Dihydro-5-deaza-FADH2 | reconstitution of the apoenzyme with 50% recovery of the ativity, Km: 0.00071 | Escherichia coli | |
| 4.1.1.47 | 5-deaza-FAD | can reconstitute the apoenzyme to full activity, Km: 0.00074 mM | Escherichia coli | |
| 4.1.1.47 | FAD | coenzyme | Escherichia coli | |
| 4.1.1.47 | FAD | 1 mol of FAD per mol of dimer, Km: 0.00025 mM | Escherichia coli | |
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Release 2023.1 (January 2023)
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