Phosphopantothenoylcysteine decarboxylase

In enzymology, a phosphopantothenoylcysteine decarboxylase (EC 4.1.1.36) is an enzyme that catalyzes the chemical reaction

N-[(R)-4'-phosphopantothenoyl]-L-cysteine ${\displaystyle \rightleftharpoons }$ pantotheine 4'-phosphate + CO₂

Hence, this enzyme has one substrate, [[N-[(R)-4'-phosphopantothenoyl]-L-cysteine]], and two products, 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-[(R)-4'-phosphopantothenoyl]-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-[(R)-4'-phosphopantothenoyl]-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 1MVL, 1MVN, and 1QZU.

References[]

• Brown GM (1958). "Requirement of cytidine triphosphate for the biosynthesis of phosphopantetheine". J. Am. Chem. Soc. 80 (12): 3161. doi:10.1021/ja01545a062.
• Brown GM (February 1959). "The metabolism of pantothenic acid". The Journal of Biological Chemistry. 234 (2): 370–8. PMID 13630913.