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
- enoyl-CoA carboxylases/reductases (ECRs)[3]
References
- Iding, H.; Siegert, P.; Mesch, K.; Pohl, M. (1998). "Application of α-keto acid decarboxylases in biotransformations". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1385 (2): 307–322. doi:10.1016/S0167-4838(98)00076-4. PMID 9655924.
- "E.C.4.1.1.- Carboxy-lyases". www.biochem.ucl.ac.uk. Archived from the original on 2006-10-13. Retrieved 2006-11-08.
- Schwander, Thomas; Schada von Borzyskowski, Lennart; Burgener, Simon; Cortina, Niña Socorro; Erb, Tobias J. (2016). "A synthetic pathway for the fixation of carbon dioxide in vitro". Science. 354 (6314): 900–904. Bibcode:2016Sci...354..900S. doi:10.1126/science.aah5237. PMC 5892708. PMID 27856910.
External links
- Carboxy-Lyases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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