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Literature summary for 2.6.1.45 extracted from
- Reaction of serine-glyoxylate aminotransferase with the alternative substrate ketomalonate indicates rate-limiting protonation of a quinonoid intermediate (2005), Biochemistry, 44, 15930-15936.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli strain HB101 | Hyphomicrobium methylovorum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Hyphomicrobium methylovorum | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni-NTA column chromatography | Hyphomicrobium methylovorum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-serine + 2-oxomalonate | - |
Hyphomicrobium methylovorum | 3-hydroxypyruvate + 2-aminomalonate | - |
? |  |
| L-serine + glyoxylate | - |
Hyphomicrobium methylovorum | 3-hydroxypyruvate + glycine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| serine-glyoxylate aminotransferase | - |
Hyphomicrobium methylovorum |
| SGAT | - |
Hyphomicrobium methylovorum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Hyphomicrobium methylovorum | |
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Release 2023.1 (January 2023)
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