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Literature summary for 2.8.3.16 extracted from

  • Ricagno, S.; Jonsson, S.; Richards, N.; Lindqvist, Y.
    Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer (2003), EMBO J., 22, 3210-3219.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
selenocysteine-substituted enzyme mutant, expression in Escherichia coli Oxalobacter formigenes

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant selenocysteine-substituted enzyme, hanging drop method, protein solution: 4.75 mg/ml, 25 mM MES, pH 6.2, 10% glycerol, drop volume 0.002 ml, reservoir solution: 100 mM HEPES, pH 7.5, 26% polyethylene glycol 4000, 0.5 M MgCl2, 291 K, 2 weeks, X-ray diffraction structure determination and analysis Oxalobacter formigenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
formyl-CoA + oxalate Oxalobacter formigenes activation-decarboxylation reaction in the catabolism of oxalic acid, degradation and detoxification in mammalian intestinal flora formate + oxalyl-CoA
-
?

Organism

Organism UniProt Comment Textmining
Oxalobacter formigenes O06644 gene frc
-

Purification (Commentary)

Purification (Comment) Organism
selenocysteine-substituted enzyme mutant, recombinant from Escherichia coli, to homogeneity Oxalobacter formigenes

Reaction

Reaction Comment Organism Reaction ID
formyl-CoA + oxalate = formate + oxalyl-CoA CoA binding sites are located at the interface between the subunits of the dimer Oxalobacter formigenes
formyl-CoA + oxalate = formate + oxalyl-CoA reaction mechanism, no classical ping-pong mechanism Oxalobacter formigenes

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formyl-CoA + oxalate
-
Oxalobacter formigenes formate + oxalyl-CoA
-
?
formyl-CoA + oxalate activation-decarboxylation reaction in the catabolism of oxalic acid, degradation and detoxification in mammalian intestinal flora Oxalobacter formigenes formate + oxalyl-CoA
-
?
additional information no activity with acetate or malonate Oxalobacter formigenes ?
-
?
succinyl-CoA + oxalate
-
Oxalobacter formigenes succinate + oxalyl-CoA
-
?

Subunits

Subunits Comment Organism
dimer enzyme monomers are tightly interacting and are interlocked, three-dimensional crystal structure analysis Oxalobacter formigenes