Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Fontenot, E.M.; Ezelle, K.E.; Gabreski, L.N.; Giglio, E.R.; McAfee, J.M.; Mills, A.C.; Qureshi, M.N.; Salmon, K.M.; Toyota, C.G.
    YfdW and YfdU are required for oxalate-induced acid tolerance in Escherichia coli K-12 (2013), J. Bacteriol., 195, 1446-1455.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.8 Oxalyl-CoA Escherichia coli
-
 Formyl-CoA + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.8 Escherichia coli
-
 strains K-12 BW25113 and MG1655, gene yfdU
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.8 Oxalyl-CoA
-
 Escherichia coli Formyl-CoA + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.8 yfdU
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
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 Escherichia coli
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 Escherichia coli