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.
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
- 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
External links
- Carboxy-Lyases at the US National Library of Medicine Medical Subject Headings (MeSH)
References
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