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In enzymology, a phosphopantothenoylcysteine decarboxylase () is an enzyme that catalyzes the chemical reaction :N-()-L-cysteine pantotheine 4'-phosphate + CO2 Hence, this enzyme has one substrate, )-L-cysteine" TITLE="N-()-L-cysteine">N-()-L-cysteine, and two products, pantotheine 4'-phosphate and CO2. This enzyme belongs to the family of lyases, to be specific the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is N-()-L-cysteine carboxy-lyase (pantotheine-4'-phosphate-forming). Other names in common use include 4-phosphopantotheoylcysteine decarboxylase, 4-phosphopantothenoyl-L-cysteine decarboxylase, PPC-decarboxylase, and N-()-L-cysteine carboxy-lyase. This enzyme participates in coenzyme A (CoA) biosynthesis from pantothenic acid. ==Structural studies== As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and . 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「phosphopantothenoylcysteine decarboxylase」の詳細全文を読む スポンサード リンク
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