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Literature summary extracted from

  • Selmer, T.; Buckel, W.
    Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentans. Implications for the mechanism of CoA-ester hydrolysis (1999), J. Biol. Chem., 274, 20772-20778.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.3.12 overexpression of wild-type and betaE54D mutant enzyme in Escherichia coli 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 E54D mutation in the subunit GctB Acidaminococcus fermentans
2.8.3.12 E54D replacement of the catalytic glutamate by aspartate converts the mutant enzyme to a thiol ester hydrolase Acidaminococcus fermentans
2.8.3.12 E54N mutation in the subunit GctB, inactive mutant Acidaminococcus fermentans
2.8.3.12 E54Q mutation in the subunit GctB Acidaminococcus fermentans
2.8.3.12 E54Q 1% as active as wild-type enzyme, by incubating with both substrates for 20 h at room temperature, glutamine is completely converted to glutamate yielding a fully active CoA-transferase Acidaminococcus fermentans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.3.12 29018
-
 alpha4beta4, 4 * 35573 + 4 * 29018, MALDI-TOF mass spectrometry Acidaminococcus fermentans
2.8.3.12 35573
-
 alpha4beta4, 4 * 35573 + 4 * 29018, MALDI-TOF mass spectrometry 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
-
 r

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.3.12 recombinant wild-type and betaE54D mutant enzyme, expressed in Escherichia coli Acidaminococcus fermentans

Reaction

EC Number Reaction Comment Organism Reaction ID
2.8.3.12 acetyl-CoA + (E)-glutaconate = acetate + glutaconyl-1-CoA reaction mechanism Acidaminococcus fermentans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.3.12 acetyl-CoA + (R)-2-hydroxyglutarate
-
 Acidaminococcus fermentans acetate + (R)-2-hydroxyglutaryl-1-CoA
-
 r
2.8.3.12 acetyl-CoA + (R)-2-hydroxyglutarate in the course of glutamate fermentation Acidaminococcus fermentans acetate + (R)-2-hydroxyglutaryl-CoA
-
 r
2.8.3.12 glutaryl-CoA + acetate exchange of oxygen atoms between the substrates and the catalytic residue betaE-54, exchange is site-specific, reversible and requires both substrates, catalytic mechanism Acidaminococcus fermentans glutarate + acetyl-CoA
-
 r
2.8.3.12 additional information wild-type enzyme has significant hydrolase activity using acetyl-CoA as substrate, but no hydrolysis of glutaryl-CoA Acidaminococcus fermentans ?
-
 ?
2.8.3.12 additional information catalytic residue is E-54 of subunit B, catalytic mechanism Acidaminococcus fermentans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.8.3.12 octamer alpha4beta4, 4 * 35573 + 4 * 29018, MALDI-TOF mass spectrometry Acidaminococcus fermentans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.8.3.12 25
-
 assay at, hydrolase activity Acidaminococcus fermentans
2.8.3.12 37
-
 assay at, CoA-transferase activity Acidaminococcus fermentans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.8.3.12 7
-
 assay at Acidaminococcus fermentans