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Literature summary extracted from

  • Mullins, E.A.; Starks, C.M.; Francois, J.A.; Sael, L.; Kihara, D.; Kappock, T.J.
    Formyl-coenzyme A (CoA):oxalate CoA-transferase from the acidophile Acetobacter aceti has a distinctive electrostatic surface and inherent acid stability (2012), Protein Sci., 21, 686-696.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.3.16 expressed in Escherichia coli BL21(DE3) cells Acetobacter aceti

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.3.16 His6-tagged enzyme, in complex with CoA, hanging drop vapor diffusion method, using 24% (w/v) PEG 4000 and 100 mM bicine, pH 8.8 Acetobacter aceti

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8.3.16 0.0034
-
 formyl-CoA in 50 mM potassium phosphate, pH 6.7, at 25°C Acetobacter aceti
2.8.3.16 1.11
-
 oxalate in 50 mM potassium phosphate, pH 6.7, at 25°C Acetobacter aceti

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.8.3.16 cytoplasm
-
 Acetobacter aceti 5737
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.3.16 47000
-
 2 * 47000, His6-tagged enzyme, SDS-PAGE Acetobacter aceti
2.8.3.16 49610
-
 2 * 49610, electrospray ionization mass spectrometry Acetobacter aceti
2.8.3.16 83000
-
 His6-tagged enzyme, gel filtration Acetobacter aceti
2.8.3.16 99000
-
 calculated from amino acid sequence Acetobacter aceti

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 Acetobacter aceti
-
 formate + oxalyl-CoA
-
 ?
2.8.3.16 formyl-CoA + oxalate Acetobacter aceti 1023
-
 formate + oxalyl-CoA
-
 ?
4.1.1.8 Oxalyl-CoA Acetobacter aceti
-
 Formyl-CoA + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.3.16 Acetobacter aceti A9X6P7
-
-
2.8.3.16 Acetobacter aceti 1023 A9X6P7
-
-
4.1.1.8 Acetobacter aceti
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.3.16 iminodiacetate-Ni2+ Sepharose column chromatography Acetobacter aceti

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.16 formyl-CoA + oxalate
-
 Acetobacter aceti formate + oxalyl-CoA
-
 ?
2.8.3.16 formyl-CoA + oxalate
-
 Acetobacter aceti 1023 formate + oxalyl-CoA
-
 ?
4.1.1.8 Oxalyl-CoA
-
 Acetobacter aceti Formyl-CoA + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
2.8.3.16 homodimer 2 * 47000, His6-tagged enzyme, SDS-PAGE Acetobacter aceti
2.8.3.16 homodimer 2 * 49610, electrospray ionization mass spectrometry Acetobacter aceti

Synonyms

EC Number Synonyms Comment Organism
2.8.3.16 FCOCT
-
 Acetobacter aceti
2.8.3.16 formyl-CoA:oxalate CoA-transferase
-
 Acetobacter aceti
2.8.3.16 uctB
-
 Acetobacter aceti
4.1.1.8 OXC
-
 Acetobacter aceti

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.8.3.16 4.5
-
 formyl-CoA in 50 mM potassium phosphate, pH 6.7, at 25°C Acetobacter aceti
2.8.3.16 5
-
 oxalate in 50 mM potassium phosphate, pH 6.7, at 25°C Acetobacter aceti

Expression

EC Number Organism Comment Expression
2.8.3.16 Acetobacter aceti the enzyme is induced by acid stress up

General Information

EC Number General Information Comment Organism
4.1.1.8 physiological function bacterial formyl-CoA:oxalate CoA-transferase and oxalyl-CoA decarboxylase work in tandem to perform a proton-consuming decarboxylation that has been suggested to have a role in generalized acid resistance Acetobacter aceti

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.8.3.16 4.5
-
 oxalate in 50 mM potassium phosphate, pH 6.7, at 25°C Acetobacter aceti
2.8.3.16 1300
-
 formyl-CoA in 50 mM potassium phosphate, pH 6.7, at 25°C Acetobacter aceti