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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 glyoxylate | Escherichia coli | - |
tartronate semialdehyde + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 glyoxylate | - |
Escherichia coli | tartronate semialdehyde + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GCL | - |
Escherichia coli |
Glyoxylate carboligase | - |
Escherichia coli |
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 |