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Literature summary extracted from

  • Mullins, E.A.; Sullivan, K.L.; Kappock, T.J.
    Function and X-ray crystal structure of Escherichia coli YfdE (2013), PLoS ONE, 8, e67901.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.3.19 expressed in Escherichia coli BL21(DE3) or C41(DE3) cells Escherichia coli
4.1.1.8 gene yfdU Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.3.19 hanging drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.5, 0.2 M MgCl2, and 20% (w/v) PEG 8000 Escherichia coli
2.8.3.19 hanging drop vapor diffusion method, using 0.1 M Tris-NHCl, pH 8.5, 0.2 M MgCl2, and 20% (w/v) PEG 8000 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8.3.19 0.017
-
 acetyl-CoA at pH 6.7 and 25°C Escherichia coli
2.8.3.19 22
-
 oxalate at pH 6.7 and 25°C Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.3.19 acetate + oxalyl-CoA Escherichia coli
-
 acetyl-CoA + oxalate
-
 ?
4.1.1.8 Oxalyl-CoA Escherichia coli
-
 Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA Oxalobacter formigenes
-
 Formyl-CoA + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.3.19 Escherichia coli P76518
-
-
4.1.1.8 Escherichia coli
-
 gene yfdU is encoded in the yfdXWUVE operon
-
4.1.1.8 Oxalobacter formigenes
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.3.19 ammonium sulfate precipitation, DEAE Sepharose column chromatography, and Cibacron Blue 3GA column chromatography Escherichia coli
2.8.3.19 ammonium sulfate precipitation, Ni-NTA column chromatography, and Cibacron Blue 3GA column chromatography Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.8.3.19 9.5
-
 at pH 6.7 and 25°C Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.19 acetate + oxalyl-CoA
-
 Escherichia coli acetyl-CoA + oxalate
-
 ?
2.8.3.19 additional information the enzyme shows low activity with formyl-CoA and acetate or oxalate, no activity with acetyl-CoA and succinate, formyl-CoA and succinate, or succinyl-CoA and oxalate Escherichia coli ?
-
 ?
2.8.3.19 oxalate + acetyl-CoA
-
 Escherichia coli oxalyl-CoA + acetate
-
 r
4.1.1.8 Oxalyl-CoA
-
 Escherichia coli Formyl-CoA + CO2
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Oxalobacter formigenes Formyl-CoA + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
2.8.3.19 dimer x-ray crystallography Escherichia coli
2.8.3.19 homodimer x-ray crystallography Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.8.3.19 acetyl-CoA:oxalate CoA transferase
-
 Escherichia coli
2.8.3.19 acetyl-CoA:oxalate CoA-transferase
-
 Escherichia coli
2.8.3.19 ACOCT
-
 Escherichia coli
2.8.3.19 YfdE
-
 Escherichia coli
4.1.1.8 OXC
-
 Escherichia coli
4.1.1.8 OXC
-
 Oxalobacter formigenes
4.1.1.8 yfdU
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.8.3.19 11
-
 acetyl-CoA at pH 6.7 and 25°C Escherichia coli
2.8.3.19 15
-
 oxalate at pH 6.7 and 25°C Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.8 thiamine diphosphate dependent on Escherichia coli
4.1.1.8 thiamine diphosphate dependent on Oxalobacter formigenes

Expression

EC Number Organism Comment Expression
4.1.1.8 Escherichia coli transcription of the yfdXWUVE operon containing yfdU, which encodes the enzyme, is activated by the acid-response regulator EvgA up

General Information

EC Number General Information Comment Organism
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 Escherichia coli
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 Oxalobacter formigenes

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.8.3.19 0.68
-
 oxalate at pH 6.7 and 25°C Escherichia coli
2.8.3.19 650
-
 acetyl-CoA at pH 6.7 and 25°C Escherichia coli