Carboxy-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, beta-keto acids and alpha-keto acids[1].
Contents |
[edit] 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
[edit] Examples
- Aromatic-L-amino-acid decarboxylase
- Glutamate decarboxylase
- Ornithine decarboxylase
- Pyruvate decarboxylase
- RuBisCO
- Uridine monophosphate synthetase
- Uroporphyrinogen III decarboxylase
[edit] See also
[edit] External links
[edit] References
Active site - Binding site - Catalytically perfect enzyme - Coenzyme - Cofactor - EC number - Enzyme catalysis - Enzyme kinetics - Enzyme inhibitor - Lineweaver-Burk plot - Michaelis-Menten kinetics
EC1 Oxidoreductases,O+R+D/list (alcohol oxidoreductases, CH-CH oxidoreductases, peroxidase, oxygenase) - EC2 Transferases/list (methyltransferase, acyltransferase, glycosyltransferase, transaminase, phosphotransferase, polymerase, kinase) - EC3 Hydrolases/list (esterase, DNA glycosylases, glycosidase, protease, acid anhydride hydrolases) - EC4 Lyases/list (carboxy-lyases, aldolase, dehydratase, synthase, adenylate cyclase, guanylate cyclase) - EC5 Isomerases/list (mutase, topoisomerase) - EC6 Ligases/list (DNA ligase, aminoacyl tRNA synthetase)