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Literature summary for 4.1.1.8 extracted from
- Formyl-coenzyme A (CoA):oxalate CoA-transferase from the acidophile Acetobacter aceti has a distinctive electrostatic surface and inherent acid stability (2012), Protein Sci., 21, 686-696.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Oxalyl-CoA | Acetobacter aceti | - |
Formyl-CoA + CO2 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acetobacter aceti | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Oxalyl-CoA | - |
Acetobacter aceti | Formyl-CoA + CO2 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| OXC | - |
Acetobacter aceti |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | bacterial formyl-CoA:oxalate CoA-transferase and oxalyl-CoA decarboxylase work in tandem to perform a proton-consuming decarboxylation that has been suggested to have a role in generalized acid resistance | Acetobacter aceti |
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Release 2023.1 (January 2023)
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