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Literature summary for 4.1.1.47 extracted from
- Reaction mechanisms of thiamin diphosphate enzymes: new insights into the role of a conserved glutamate residue (2009), FEBS J., 276, 2447-2453.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| V51D | replacement of Val51 by an amino acid with a carboxylate in its side chain (glutamate or aspartate) has striking and significant effects, V51D variant of glyoxylate carboligase undergoes proton exchange at a rate 6fold higher than the wild-type enzyme | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 glyoxylate | Escherichia coli | - |
tartronate semialdehyde + CO2 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 glyoxylate | - |
Escherichia coli | tartronate semialdehyde + CO2 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GCL | - |
Escherichia coli |
| Glyoxylate carboligase | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thiamine diphosphate | the structure of glyoxylate carboligase reveals that there is no glutamate in a position to interact with N1 of thiamine diphosphate, the position homologous to the conserved glutamate is occupied by Val51 | Escherichia coli | |
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Release 2023.1 (January 2023)
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