EC Number   |
General Information |
Reference |
|---|
   4.1.1.8 | malfunction |
the absence of the YfdU protein increases the cell vulnerability to low pH, oxalic acid, or both. Oxalate-dependent pH tolerance of the yfdU-deletion strain is clearly impaired, glutamate-dependent acid resistance is not impaired by deletion of the either yfdW or yfdU |
727769 |
| 4.1.1.8 | 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 |
726452 |
| 4.1.1.8 | physiological function |
proteins YfdW and YfdU are necessary and sufficient for oxalate-induced protection against a subsequent acid challenge. EvgA activates proton-consuming amino acid decarboxylases during strong acid resistance responses. Oxalate catabolism counteracts acid stress by oxalyl-CoA decarboxylation. Oxalate elicits a moderate, rpoS-independent acid tolerance response that requires both yfdW and yfdU in Escherichia coli. But product(s) of the yfdXWUVE operon appear to have no essential role in general acid stress responses and may serve a more specialized function |
726342 |
| 4.1.1.8 | physiological function |
the commensal bacterium Oxalobacter formigenes consumes oxalate by converting it to oxalyl-CoA, which is decarboxylated by oxalyl-CoA decarboxylase |
726342 |
| 4.1.1.8 | physiological function |
the enzymes YfdW, a formyl coenzyme A (CoA) transferase, and YfdU, an oxalyl-CoA decarboxylase, are required for oxalate adaptation but not during challenge in minimal challenge medium. YfdW and YfdU are part of an AR2-like system where oxalate is brought into the cell by YhjX and decarboxylated in a reaction similar to that catalyzed by GadA/B in the challenge medium. Oxalate induces an acid tolerance response when Escherichia coli cells are adapted at pH 5.5 and the enzymes YfdW and YfdU, but not YhjX, are required for this response, overview |
727769 |
