Literature summary 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.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.8.3.16 |
selenocysteine-substituted enzyme mutant, expression in Escherichia coli |
Oxalobacter formigenes |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.8.3.16 |
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)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.8.3.16 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.8.3.16 |
Oxalobacter formigenes |
O06644 |
gene frc |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.8.3.16 |
selenocysteine-substituted enzyme mutant, recombinant from Escherichia coli, to homogeneity |
Oxalobacter formigenes |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
2.8.3.16 |
formyl-CoA + oxalate = formate + oxalyl-CoA |
CoA binding sites are located at the interface between the subunits of the dimer |
Oxalobacter formigenes |
|
2.8.3.16 |
formyl-CoA + oxalate = formate + oxalyl-CoA |
reaction mechanism, no classical ping-pong mechanism |
Oxalobacter formigenes |
|
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.8.3.16 |
formyl-CoA + oxalate |
- |
Oxalobacter formigenes |
formate + oxalyl-CoA |
- |
? |
|
2.8.3.16 |
formyl-CoA + oxalate |
activation-decarboxylation reaction in the catabolism of oxalic acid, degradation and detoxification in mammalian intestinal flora |
Oxalobacter formigenes |
formate + oxalyl-CoA |
- |
? |
|
2.8.3.16 |
additional information |
no activity with acetate or malonate |
Oxalobacter formigenes |
? |
- |
? |
|
2.8.3.16 |
succinyl-CoA + oxalate |
- |
Oxalobacter formigenes |
succinate + oxalyl-CoA |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.8.3.16 |
dimer |
enzyme monomers are tightly interacting and are interlocked, three-dimensional crystal structure analysis |
Oxalobacter formigenes |