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Literature summary extracted from

  • Mack, M.; Buckel, W.
    Identification of glutamate beta54 as the covalent-catalytic residue in the active site of glutaconate CoA-transferase from Acidaminococcus fermentans (1995), FEBS Lett., 357, 145-148.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.3.12 wild-type and mutant genes gctA and gctB encoding the two subunits GctA and GctB are cloned and expressed together in Escherichia coli XL1-Blue Acidaminococcus fermentans

Protein Variants

EC Number Protein Variants Comment Organism
2.8.3.12 E54A mutation in the subunit GctB, inactive mutant Acidaminococcus fermentans
2.8.3.12 E54A 0.02% as active as wild-type enzyme Acidaminococcus fermentans
2.8.3.12 E54D mutation in the subunit GctB Acidaminococcus fermentans
2.8.3.12 E54D above 7% as active as wild-type enzyme, mutant with changed catalytic mechanism without CoASH intermediate, the Escherichia coli strain producing mutant enzyme shows a lower growth rate and reduced amount of recombinant enzyme Acidaminococcus fermentans
2.8.3.12 E54Q mutation in the subunit GctB Acidaminococcus fermentans
2.8.3.12 E54Q mutant activity increases from 1% to almost 100% upon incubation with acetyl-CoA and glutaconate at 37°C within 40 h, the substrates induce the conversion of the mutant glutamine residue into the glutamate residue of the wild-type enzyme Acidaminococcus fermentans
2.8.3.12 E64A mutation in the subunit GctB, 30% as active as wild-type enzyme Acidaminococcus fermentans

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.8.3.12 NaBH4 strong Acidaminococcus fermentans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.3.12 29000
-
 alpha4beta4, 4 * 36000 + 4 * 29000, GctA and GctB, SDS-PAGE Acidaminococcus fermentans
2.8.3.12 36000
-
 alpha4beta4, 4 * 36000 + 4 * 29000, GctA and GctB, SDS-PAGE Acidaminococcus fermentans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.3.12 acetyl-CoA + (R)-2-hydroxyglutarate Acidaminococcus fermentans in the course of glutamate fermentation acetate + (R)-2-hydroxyglutaryl-CoA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.3.12 Acidaminococcus fermentans
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.8.3.12 additional information
-
-
 Acidaminococcus fermentans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.12 acetyl-CoA + (E)-glutaconate
-
 Acidaminococcus fermentans acetate + glutaconyl-1-CoA
-
 ?
2.8.3.12 acetyl-CoA + (R)-2-hydroxyglutarate
-
 Acidaminococcus fermentans acetate + (R)-2-hydroxyglutaryl-1-CoA
-
 ?
2.8.3.12 acetyl-CoA + (R)-2-hydroxyglutarate in the course of glutamate fermentation Acidaminococcus fermentans acetate + (R)-2-hydroxyglutaryl-CoA
-
 ?
2.8.3.12 additional information residue E-54 of the subunit GctB is directly involved in catalysis by formation of a CoASH ester intermediate Acidaminococcus fermentans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.8.3.12 octamer alpha4beta4, 4 * 36000 + 4 * 29000, GctA and GctB, SDS-PAGE Acidaminococcus fermentans