EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  4.1.3.B3 | 4-carboxy-4-hydroxy-2-oxoadipate |
- |
Pseudomonas putida |
pyruvate + oxaloacetate |
- |
r |
| 4.1.3.B3 | 4-carboxy-4-hydroxy-2-oxoadipate |
- |
Pseudomonas putida |
oxaloacetate + pyruvate |
- |
? |
| 4.1.3.B3 | 4-carboxy-4-hydroxy-2-oxoadipate |
- |
Comamonas testosteroni |
oxaloacetate + pyruvate |
- |
? |
| 4.1.3.B3 | 4-carboxy-4-hydroxy-2-oxoadipate |
- |
Comamonas testosteroni CNB-1 |
oxaloacetate + pyruvate |
- |
? |
| 4.1.3.B3 | more |
the bifunctional enzyme PmdF shows obvious aldolase activity when 4-carboxy-4-hydroxy-2-oxoadipate is used as substrate and obvious oxalacetate decarboxylase activity when oxaloacetate is used as substrate |
Comamonas testosteroni |
? |
- |
? |
| 4.1.3.B3 | more |
the enzyme is a class II, divalent metal ion-dependent, pyruvate aldolase that catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate and 4-carboxy-4-hydroxy-2-oxoadipate into two molecules of pyruvate in the former and a molecule of each pyruvate and oxaloacetate in the latter, cf. EC 4.1.3.17. The enzyme also contains a secondary oxaloacetate decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retroaldol and decarboxylase reactions |
Pseudomonas putida |
? |
- |
? |
| 4.1.3.B3 | more |
the bifunctional enzyme PmdF shows obvious aldolase activity when 4-carboxy-4-hydroxy-2-oxoadipate is used as substrate and obvious oxalacetate decarboxylase activity when oxaloacetate is used as substrate |
Comamonas testosteroni CNB-1 |
? |
- |
? |
