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arginine decarboxylase : ウィキペディア英語版 | arginine decarboxylase
In enzymology, an arginine decarboxylase () is an enzyme that catalyzes the chemical reaction :L-arginine agmatine + CO2 Hence, this enzyme has one substrate, L-arginine, and two products, agmatine 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 L-arginine carboxy-lyase (agmatine-forming). Other names in common use include SpeA, and L-arginine carboxy-lyase. This enzyme participates in urea cycle and metabolism of amino groups and glutamate metabolism. It employs one cofactor, pyridoxal phosphate. ==Structural studies==
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
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