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Literature summary extracted from
- Amino acid sequence of the pyruvate and the glyoxylate active-site lysine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase (1986), J. Biol. Chem., 261, 11049-11055.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.3.42 | glyoxylate | substrate inhibition. Glyoxylate competes for, and inhibits aldolase activity by reacting with, the one active-site lysine residue/subunit | Escherichia coli |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.3.42 | Escherichia coli | P0A955 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.3.42 | (4S)-4-hydroxy-2-oxoglutarate | - |
Escherichia coli | pyruvate + glyoxylate | - |
r | |
| 4.1.3.42 | additional information | enzyme binds any one of its substrates 2-keto-4-hydroxyglutarate, pyruvate, or glyoxylate in a competitive manner | Escherichia coli | ? | - |
? | |
| 4.1.3.42 | pyruvate + glyoxylate | - |
Escherichia coli | (4S)-4-hydroxy-2-oxoglutarate | - |
r | |
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