Carboxy-lyases
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, beta-keto 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
See also
References
- ^ http://www.expasy.org/cgi-bin/get-entries?KW=Decarboxylase
- ^ "E.C.4.1.1.- Carboxy-lyases". www.biochem.ucl.ac.uk. Archived from the original on 2006-10-13. Retrieved 2006-11-08.
External links
- Carboxy-Lyases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
