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].
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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
- Aromatic-L-amino-acid decarboxylase
- Glutamate decarboxylase
- Histidine decarboxylase
- Ornithine decarboxylase
- Pyruvate decarboxylase
- RuBisCO
- Uridine monophosphate synthetase
- Uroporphyrinogen III decarboxylase
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| Topics | Active site - Allosteric regulation - Binding site - Catalytically perfect enzyme - Coenzyme - Cofactor - Cooperativity - EC number Enzyme catalysis - Enzyme inhibitor - Enzyme kinetics - Lineweaver-Burk plot - Michaelis-Menten kinetics - List of enzymes |
| Types | EC1 Oxidoreductases/list - EC2 Transferases/list - EC3 Hydrolases/list - EC4 Lyases/list - EC5 Isomerases/list - EC6 Ligases/list |