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Literature summary for 4.1.1.8 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
Search for more literature for 4.1.1.8

Cloned(Commentary)

Cloned (Comment) Organism
gene yfdU Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 gene yfdU is encoded in the yfdXWUVE operon
-
Oxalobacter formigenes
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Oxalyl-CoA
-
 Escherichia coli Formyl-CoA + CO2
-
 ?
Oxalyl-CoA
-
 Oxalobacter formigenes Formyl-CoA + CO2
-
 ?

Synonyms

Synonyms Comment Organism
OXC
-
 Escherichia coli
OXC
-
 Oxalobacter formigenes
yfdU
-
 Escherichia coli

Cofactor

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

Expression

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

General Information

General Information Comment Organism
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
physiological function the commensal bacterium Oxalobacter formigenes consumes oxalate by converting it to oxalyl-CoA, which is decarboxylated by oxalyl-CoA decarboxylase Oxalobacter formigenes