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Carboxy-lyases

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Class of enzymes, carbon–carbon 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 and alpha-keto acids.

Classification and nomenclature

Carboxy-lyases are categorized under EC number 4.1.1. Usually, they are named after the substrate whose decarboxylation they catalyze, for example pyruvate decarboxylase catalyzes the decarboxylation of pyruvate.

Examples

See also

References

  1. 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.
  2. "E.C.4.1.1.- Carboxy-lyases". www.biochem.ucl.ac.uk. Archived from the original on 2006-10-13. Retrieved 2006-11-08.
  3. 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.

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External links

Carbon–carbon lyases (EC 4.1)
4.1.1: Carboxy-lyases
4.1.2: Aldehyde-lyases
4.1.3: Oxo-acid-lyases
4.1.99: Other
Enzymes
Activity
Regulation
Classification
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