Sulfinoalanine decarboxylase | |||||||||
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Identifiers | |||||||||
EC no. | 4.1.1.29 | ||||||||
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 sulfinoalanine decarboxylase (EC 4.1.1.29) catalyzes the chemical reaction
Hence, this enzyme has one substrate, 3-sulfino-L-alanine (also known as Cysteine sulfinic acid), and two products, hypotaurine and CO2.
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 3-sulfino-L-alanine carboxy-lyase (hypotaurine-forming). Other names in common use include cysteine-sulfinate decarboxylase, L-cysteinesulfinic acid decarboxylase, cysteine-sulfinate decarboxylase, CADCase/CSADCase, CSAD, cysteic decarboxylase, cysteinesulfinic acid decarboxylase, cysteinesulfinate decarboxylase, sulfoalanine decarboxylase, and 3-sulfino-L-alanine carboxy-lyase. This enzyme participates in taurine metabolism. It employs one cofactor, pyridoxal phosphate.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2JIS.
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.
Alanine dehydrogenase (EC 1.4.1.1) is an enzyme that catalyzes the chemical reaction
The enzyme 2,2-dialkylglycine decarboxylase (pyruvate) (EC 4.1.1.64) catalyzes the chemical reaction
The enzyme 4-hydroxy-2-oxoglutarate aldolase catalyzes the chemical reaction
THe enzyme 6-methylsalicylate decarboxylase (EC 4.1.1.52) catalyzes the chemical reaction
The enzyme aminocarboxymuconate-semialdehyde decarboxylase (EC 4.1.1.45) catalyzes the chemical reaction
The enzyme aspartate 1-decarboxylase (EC 4.1.1.11) 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 benzoylformate decarboxylase (EC 4.1.1.7) catalyzes the following 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.
In enzymology, a glutaconyl-CoA decarboxylase (EC 4.1.1.70) is an enzyme that catalyzes the chemical reaction
The enzyme indolepyruvate decarboxylase (EC 4.1.1.74) catalyzes the chemical reaction
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The enzyme phenylalanine decarboxylase (EC 4.1.1.53) catalyzes the chemical reaction
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The enzyme prephenate dehydratase (EC 4.2.1.51) catalyzes the chemical reaction
In enzymology, a phenacrylate decarboxylase (EC 4.1.1.102) is an enzyme that catalyzes the chemical reaction