EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.3.1.226 | ethylmalonyl-CoA + (2S,5S)-carboxymethylproline + CO2 |
the substrate is an equilibrium mixture of L-glutamate semialdehyde, 5-hydroxy-L-proline and L-pyrroline-5-carboxylate. Some of the CarB variants catalyse the production of the two C6 epimers of (2S,5S)-6-ethyl-5-carboxymethylproline |
Pectobacterium carotovorum |
CoA + (2S,5S,6R)-6-ethyl-5-carboxymethylproline |
wild-type enzyme produces a 65:35 mixture of (6R)- and (6S)-epimer |
? |
2.3.1.226 | ethylmalonyl-CoA + (2S,5S)-carboxymethylproline + CO2 |
the substrate is an equilibrium mixture of L-glutamate semialdehyde, 5-hydroxy-L-proline and L-pyrroline-5-carboxylate. Some of the CarB variants catalyse the production of the two C6 epimers of (2S,5S)-6-ethyl-5-carboxymethylproline |
Pectobacterium carotovorum |
CoA + (2S,5S,6S)-6-ethyl-5-carboxymethylproline |
wild-type enzyme produces a 65:35 mixture of (6R)- and (6S)-epimer |
? |
2.3.1.226 | ethylmalonyl-CoA + L-2-aminoadipate semialdehyde |
activity with mutant enzymes W79F, W79F/M108A and W79F/M108V. mutant W79A: epimeric ethylmalonylCoA produces solely (2S,6S,7S)-(2S,6S)-carboxymethylpipecolic acid via reaction of (2R)-ethylmalonyl-CoA, whereas incubation of (2S)-ethylmalonylCoA and L-2-aminoadipate semialdehyde results in no detectable production of 7-ethyl-(2S,6S)-carboxymethylpipecolic acid |
Pectobacterium carotovorum |
CoA + (2S,6S,7R)-7-ethyl-carboxymethylpipecolic acid |
- |
? |
2.3.1.226 | ethylmalonyl-CoA + L-2-aminoadipate semialdehyde |
activity with mutant enzymes W79F, W79F/M108A and W79F/M108V. mutant W79A: epimeric ethylmalonylCoA produces solely (2S,6S,7S)-(2S,6S)-carboxymethylpipecolic acid via reaction of (2R)-ethylmalonyl-CoA, whereas incubation of (2S)-ethylmalonylCoA and L-2-aminoadipate semialdehyde results in no detectable production of 7-ethyl-(2S,6S)-carboxymethylpipecolic acid |
Pectobacterium carotovorum |
CoA + (2S,6S,7S)-7-ethyl-carboxymethylpipecolic acid |
- |
? |
2.3.1.226 | malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O |
- |
Pectobacterium carotovorum |
CoA + (2S,5S)-5-carboxymethylproline + CO2 |
- |
? |
2.3.1.226 | malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O |
the enzyme catalyzes committed step in the biosynthesis of (5R)-carbapenem-3-carboxylic acid, the simplest of the medicinally important carbapenem antibiotics |
Pectobacterium carotovorum |
CoA + (2S,5S)-5-carboxymethylproline + CO2 |
- |
? |
2.3.1.226 | malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O |
acetyl-CoA is not a substrate |
Pectobacterium carotovorum |
CoA + (2S,5S)-5-carboxymethylproline + CO2 |
- |
? |
2.3.1.226 | malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O |
CarB is a member of the crotonase superfamily of enzymes. In addition to decarboxylation and thioester hydrolysis steps, it catalyzes C-C bond formation leading to a substituted heterocycle. Mechanistic studies show that C-C bond formation by CarB most probably occurs by reaction of P5C with an oxy-anion stabilized enolate, and thioester hydrolysis most probably proceeds by direct attack of an activated water molecule |
Pectobacterium carotovorum |
CoA + (2S,5S)-5-carboxymethylproline + CO2 |
- |
? |
2.3.1.226 | malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O |
the substrate is an equilibrium mixture of L-glutamate semialdehyde, 5-hydroxy-L-proline and L-pyrroline-5-carboxylate |
Pectobacterium carotovorum |
CoA + (2S,5S)-5-carboxymethylproline + CO2 |
- |
? |
2.3.1.226 | malonyl-CoA + (S)-1-pyrroline-5-carboxylate + H2O |
- |
Pectobacterium carotovorum GS101 |
CoA + (2S,5S)-5-carboxymethylproline + CO2 |
- |
? |