EC Number | Cloned (Comment) | Organism |
---|---|---|
2.8.3.12 | overexpression of wild-type and betaE54D mutant enzyme in Escherichia coli | Acidaminococcus fermentans |
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 |
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 |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.8.3.12 | Acidaminococcus fermentans | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.8.3.12 | recombinant wild-type and betaE54D mutant enzyme, expressed in Escherichia coli | Acidaminococcus fermentans |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.8.3.12 | acetyl-CoA + (E)-glutaconate = acetate + glutaconyl-1-CoA | reaction mechanism | Acidaminococcus fermentans |
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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.8.3.12 | octamer | alpha4beta4, 4 * 35573 + 4 * 29018, MALDI-TOF mass spectrometry | Acidaminococcus fermentans |
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 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.8.3.12 | 7 | - |
assay at | Acidaminococcus fermentans |