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Literature summary extracted from

  • Berthold, C.L.; Toyota, C.G.; Richards, N.G.; Lindqvist, Y.
    Reinvestigation of the catalytic mechanism of formyl-CoA transferase, a class III CoA-transferase (2008), J. Biol. Chem., 283, 6519-6529.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.3.16 expression in Escherichia coli BL21-DE3 Oxalobacter formigenes

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.3.16 beta-aspartyl-CoA thioester intermediate is identified by x-ray crystallography Oxalobacter formigenes

Protein Variants

EC Number Protein Variants Comment Organism
2.8.3.16 G259A site-directed mutagenesis Oxalobacter formigenes
2.8.3.16 G260A site-directed mutagenesis Oxalobacter formigenes
2.8.3.16 Q17A site-directed mutagenesis Oxalobacter formigenes

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.8.3.16 Cl-
-
 Oxalobacter formigenes
2.8.3.16 coenzyme A
-
 Oxalobacter formigenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8.3.16 0.002
-
 formyl-CoA wild-type formyl-CoA transferase Oxalobacter formigenes
2.8.3.16 0.0047
-
 formyl-CoA G259A mutant formyl-CoA transferase Oxalobacter formigenes
2.8.3.16 0.018
-
 formyl-CoA G260A mutant formyl-CoA transferase Oxalobacter formigenes
2.8.3.16 0.033
-
 formyl-CoA Q17A mutant formyl-CoA transferase Oxalobacter formigenes
2.8.3.16 3.9
-
 oxalate wild-type formyl-CoA transferase Oxalobacter formigenes
2.8.3.16 12.1
-
 oxalate G259A mutant formyl-CoA transferase Oxalobacter formigenes
2.8.3.16 13.2
-
 oxalate Q17A mutant formyl-CoA transferase Oxalobacter formigenes
2.8.3.16 18
-
 oxalate G260A mutant formyl-CoA transferase 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 oxalate catabolism has a central role in Oxalobacter formigenes, where oxalate serves as vital source of energy as well as carbon formate + oxalyl-CoA
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.8.3.16 Oxalobacter formigenes O06644
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.3.16 DEAE anion exchange chromatography, Blue-Sepharose fast flow affinity chromatography, Sephadex G-250 size exclusion chromatography, and QHP anion exchange chromatography Oxalobacter formigenes

Storage Stability

EC Number Storage Stability Organism
2.8.3.16 -80°C, 25 mM sodium phosphate, pH 6.2, 300 mM NaCl, 1 mM dithiothreitol and 10% glycerol Oxalobacter formigenes

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.16 formyl-CoA + oxalate oxalate catabolism has a central role in Oxalobacter formigenes, where oxalate serves as vital source of energy as well as carbon Oxalobacter formigenes formate + oxalyl-CoA
-
 r
2.8.3.16 formyl-CoA + oxalate catalytic mechanism, beta-aspartyl-CoA thioester as intermediate Oxalobacter formigenes formate + oxalyl-CoA
-
 r

Subunits

EC Number Subunits Comment Organism
2.8.3.16 dimer identified through crystallographic freeze-trapping experiments with formyl-CoA and oxalyl-CoA in the absence of acceptor carboxylic acid Oxalobacter formigenes

Synonyms

EC Number Synonyms Comment Organism
2.8.3.16 formyl-coenzyme A transferase
-
 Oxalobacter formigenes

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.8.3.16 3
-
 Cl- chloride is a weak competitive inhibitor to oxalate Oxalobacter formigenes
2.8.3.16 16.7
-
 coenzyme A
-
 Oxalobacter formigenes