Carboxy-lyases
Class of enzymes, carbon–carbon lyases
From Wikipedia, the free encyclopedia
Carboxy-lyases, also known as decarboxylases, are carbon–carbon lyases that add or remove a carboxyl group from organic compounds. These enzymes catalyze the decarboxylation of amino acids and alpha-keto acids.[1]
Classification and nomenclature
Carboxy-lyases are categorized under EC number 4.1.1.[2] Usually, they are named after the substrate whose decarboxylation they catalyze, for example pyruvate decarboxylase catalyzes the decarboxylation of pyruvate.
Examples
- Aromatic-L-amino-acid decarboxylase
- Glutamate decarboxylase
- Histidine decarboxylase
- Ornithine decarboxylase
- Phosphoenolpyruvate carboxylase
- Pyruvate decarboxylase
- RuBisCO – the only carboxylase that leads to a net fixation of carbon dioxide
- Uridine monophosphate synthetase
- Uroporphyrinogen III decarboxylase
- enoyl-CoA carboxylases/reductases (ECRs)[3]
