This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-aspartate 1-carboxy-lyase (beta-alanine-forming). Other names in common use include aspartate alpha-decarboxylase, L-aspartate alpha-decarboxylase, aspartic alpha-decarboxylase, and L-aspartate 1-carboxy-lyase. This enzyme participates in alanine and aspartate metabolism and beta-alanine metabolism.
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.
The enzyme 2,2-dialkylglycine decarboxylase (pyruvate) (EC 4.1.1.64) catalyzes the chemical reaction
The enzyme 3-dehydro-L-gulonate-6-phosphate decarboxylase (EC 4.1.1.85) catalyzes the chemical reaction
The enzyme 3-oxolaurate decarboxylase (EC 4.1.1.56) catalyzes the chemical reaction
The enzyme 5-guanidino-2-oxopentanoate decarboxylase (EC 4.1.1.75) catalyzes the chemical reaction
The enzyme acetolactate decarboxylase (EC 4.1.1.5) catalyzes the chemical reaction
The enzyme aconitate decarboxylase (EC 4.1.1.6) catalyzes the chemical reaction
The enzyme aminocarboxymuconate-semialdehyde decarboxylase (EC 4.1.1.45) catalyzes the chemical reaction
In enzymology, an aspartate 4-decarboxylase (EC 4.1.1.12) is an enzyme that catalyzes the chemical reaction
The enzyme dehydro-L-gulonate decarboxylase (EC 4.1.1.34) catalyzes the chemical reaction
The enzyme diaminopimelate decarboxylase (EC 4.1.1.20) catalyzes the cleavage of carbon-carbon bonds in meso 2,6 diaminoheptanedioate to produce CO2 and L-lysine, the essential amino acid. It employs the cofactor pyridoxal phosphate, also known as PLP, which participates in numerous enzymatic transamination, decarboxylation and deamination reactions.
The enzyme hydroxyglutamate decarboxylase (EC 4.1.1.16) catalyzes the chemical reaction
The enzyme methionine decarboxylase (EC 4.1.1.57) catalyzes the chemical reaction
In enzymology, an oxalate decarboxylase (EC 4.1.1.2) is an oxalate degrading enzyme that catalyzes the chemical reaction
The enzyme phenylalanine decarboxylase (EC 4.1.1.53) catalyzes the chemical reaction
The enzyme phosphatidylserine decarboxylase (EC 4.1.1.65) catalyzes the chemical reaction
The enzyme sulfinoalanine decarboxylase (EC 4.1.1.29) catalyzes the chemical reaction
The enzyme tyrosine decarboxylase (EC 4.1.1.25) catalyzes the chemical reaction
The enzyme UDP-galacturonate decarboxylase (EC 4.1.1.67) catalyzes the chemical reaction
The enzyme UDP-glucuronate decarboxylase (EC 4.1.1.35) catalyzes the chemical reaction
References
Williamson JM, Brown GM (1979). "Purification and properties of L-Aspartate-alpha-decarboxylase, an enzyme that catalyzes the formation of beta-alanine in Escherichia coli". J. Biol. Chem. 254 (16): 8074–82. PMID381298.
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