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
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
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
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
the presence of 0.3 mM ADP results in a marginal increase in kcat and a small decrease in Km, leading to a 1.7fold higher catalytic efficiency. One molecule of ADP is bound per monomer distant from the CoA binding site
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ODC alone or in complex with either ADP or acetyl CoA, hanging drop vapor diffusion method, using 100 mM MES/NaOH, pH 6.5 and 1.5 M ammonium sulfate for ODC alone, or 100 mM MES/NaOH, pH 6.25 and 1.75 M ammonium sulfate for ADP–bound ODC, or 100 mM MES/NaOH, pH 6.0, 0.2 M sodium acetate and 5% (w/v) poly(ethylene glycol) 4000 for acetyl CoA-bound ODC
cocrystallization of wild-type OXC with 1 mM CoA, with a precipitating solution containing 0.5 M CaCl2, 0.1 M BisTris propane (2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl) propane-1,3-diol), pH 6.5, and 26% polyethylene glycol 550 monomethyl ether
recombinant, hanging drop vapour-diffusion method, native and seleno-methionine labelled enzyme is crystallized in two different conditions resulting in two different crystal forms, one showing poor diffraction and the other merohedral twinning. Crystals in the former category belong to the tetragonal space group P4(2)2(1)2, crystals in the latter category are obtained by cocrystallization of the protein with coenzyme A, thiamine diphosphate and Mg2+. The crystal is heavily twinned with a twin ratio of 0.43
Turroni, S.; Bendazzoli, C.; Dipalo, S.C.; Candela, M.; Vitali, B.; Gotti, R.; Brigidi, P.
Oxalate-degrading activity in Bifidobacterium animalis subsp. lactis: impact of acidic conditions on the transcriptional levels of the oxalyl coenzyme A (CoA) decarboxylase and formyl-CoA transferase genes
Appl. Environ. Microbiol.
Bifidobacterium animalis subsp. lactis (B9X297), Bifidobacterium animalis subsp. lactis (C6AFP4), Bifidobacterium animalis subsp. lactis BI07 (B9X297), Bifidobacterium animalis subsp. lactis BI07 (C6AFP4), no activity in Bifidobacterium adolescentis, no activity in Bifidobacterium adolescentis ATCC 15703