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Literature summary for 2.8.3.12 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
Search for more literature for 2.8.3.12

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and betaE54D mutant enzyme in Escherichia coli Acidaminococcus fermentans

Protein Variants

Protein Variants Comment Organism
E54A mutation in the subunit GctB, inactive mutant Acidaminococcus fermentans
E54D mutation in the subunit GctB Acidaminococcus fermentans
E54D replacement of the catalytic glutamate by aspartate converts the mutant enzyme to a thiol ester hydrolase Acidaminococcus fermentans
E54N mutation in the subunit GctB, inactive mutant Acidaminococcus fermentans
E54Q mutation in the subunit GctB Acidaminococcus fermentans
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Acidaminococcus fermentans
-
-
-

Purification (Commentary)

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

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + (R)-2-hydroxyglutarate
-
 Acidaminococcus fermentans acetate + (R)-2-hydroxyglutaryl-1-CoA
-
 r
acetyl-CoA + (R)-2-hydroxyglutarate in the course of glutamate fermentation Acidaminococcus fermentans acetate + (R)-2-hydroxyglutaryl-CoA
-
 r
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
additional information wild-type enzyme has significant hydrolase activity using acetyl-CoA as substrate, but no hydrolysis of glutaryl-CoA Acidaminococcus fermentans ?
-
 ?
additional information catalytic residue is E-54 of subunit B, catalytic mechanism Acidaminococcus fermentans ?
-
 ?

Subunits

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

Temperature Optimum [°C]

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

pH Optimum

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