phenylalanine decarboxylase | |||||||||
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Identifiers | |||||||||
EC no. | 4.1.1.53 | ||||||||
CAS no. | 9075-72-3 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme phenylalanine decarboxylase (EC 4.1.1.53) catalyzes the chemical reaction
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-phenylalanine carboxy-lyase (phenylethylamine-forming). Other names in common use include L-phenylalanine decarboxylase, aromatic L-amino acid decarboxylase, and L-phenylalanine carboxy-lyase. This enzyme participates in phenylalanine metabolism. It employs one cofactor, pyridoxal phosphate.
Aromatic L-amino acid decarboxylase, also known as DOPA decarboxylase (DDC), tryptophan decarboxylase, and 5-hydroxytryptophan decarboxylase, is a lyase enzyme, located in region 7p12.2-p12.1.
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 phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic acid.:
The enzyme 2,2-dialkylglycine decarboxylase (pyruvate) (EC 4.1.1.64) catalyzes the chemical reaction
The enzyme 3-oxolaurate decarboxylase (EC 4.1.1.56) 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 branched-chain-2-oxoacid decarboxylase (EC 4.1.1.72) 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 gallate decarboxylase (EC 4.1.1.59) catalyzes the chemical reaction
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 oxalyl-CoA decarboxylase (OXC) (EC 4.1.1.8), primarily produced by the gastrointestinal bacterium Oxalobacter formigenes, catalyzes the chemical reaction
The enzyme phenylpyruvate decarboxylase (EC 4.1.1.43) catalyzes the chemical reaction
The enzyme sulfinoalanine decarboxylase (EC 4.1.1.29) catalyzes the chemical reaction
The enzyme threonine-phosphate decarboxylase (EC 4.1.1.81) catalyzes the chemical reaction
The enzyme tyrosine decarboxylase (EC 4.1.1.25) catalyzes the chemical reaction
In enzymology, a phenacrylate decarboxylase (EC 4.1.1.102) is an enzyme that catalyzes the chemical reaction