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Literature summary for 2.8.3.16 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
Search for more literature for 2.8.3.16

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
Cl-
-
 Oxalobacter formigenes
coenzyme A
-
 Oxalobacter formigenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
 formyl-CoA wild-type formyl-CoA transferase Oxalobacter formigenes
0.0047
-
 formyl-CoA G259A mutant formyl-CoA transferase Oxalobacter formigenes
0.018
-
 formyl-CoA G260A mutant formyl-CoA transferase Oxalobacter formigenes
0.033
-
 formyl-CoA Q17A mutant formyl-CoA transferase Oxalobacter formigenes
3.9
-
 oxalate wild-type formyl-CoA transferase Oxalobacter formigenes
12.1
-
 oxalate G259A mutant formyl-CoA transferase Oxalobacter formigenes
13.2
-
 oxalate Q17A mutant formyl-CoA transferase Oxalobacter formigenes
18
-
 oxalate G260A mutant formyl-CoA transferase Oxalobacter formigenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Oxalobacter formigenes O06644
-
-

Purification (Commentary)

Purification (Comment) Organism
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

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
formyl-CoA + oxalate catalytic mechanism, beta-aspartyl-CoA thioester as intermediate Oxalobacter formigenes formate + oxalyl-CoA
-
 r

Subunits

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

Synonyms

Synonyms Comment Organism
formyl-coenzyme A transferase
-
 Oxalobacter formigenes

Ki Value [mM]

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