Cloned (Comment) | Organism |
---|---|
selenocysteine-substituted enzyme mutant, expression in Escherichia coli | Oxalobacter formigenes |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Oxalobacter formigenes | O06644 | gene frc | - |
Purification (Comment) | Organism |
---|---|
selenocysteine-substituted enzyme mutant, recombinant from Escherichia coli, to homogeneity | Oxalobacter formigenes |
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 | Comment | Organism | Textmining |
---|
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 | Comment | Organism |
---|---|---|
dimer | enzyme monomers are tightly interacting and are interlocked, three-dimensional crystal structure analysis | Oxalobacter formigenes |