What is "phosphodiesterase"

n. (context enzyme English) any of a family of enzymes that catalyze the cleavage of phosphodiester links in nucleic acids

A phosphodiesterase (PDE) is any enzyme that breaks a phosphodiester bond. Usually, phosphodiesterase refers to cyclic nucleotide phosphodiesterases, which have great clinical significance and are described below. However, there are many other families of phosphodiesterases, including phospholipases C and D, autotaxin, sphingomyelin phosphodiesterase, DNases, RNases, and restriction endonucleases (which all break the phosphodiester backbone of DNA or RNA), as well as numerous less-well-characterized small-molecule phosphodiesterases.

The cyclic nucleotide phosphodiesterases comprise a group of enzymes that degrade the phosphodiester bond in the second messenger molecules cAMP and cGMP. They regulate the localization, duration, and amplitude of cyclic nucleotide signaling within subcellular domains. PDEs are therefore important regulators of signal transduction mediated by these second messenger molecules.

In enzymology, a [acyl-carrier-protein] phosphodiesterase is an enzyme that catalyzes the chemical reaction

Thus, the two substrates of this enzyme are holo-[acyl-carrier-protein] and HO, whereas its two products are 4'-phosphopantetheine and apo-[acyl-carrier-protein].

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is holo-[acyl-carrier-protein] 4'-pantetheine-phosphohydrolase. Other names in common use include ACP hydrolyase, ACP phosphodiesterase, AcpH, and [acyl-carrier-protein] 4'-pantetheine-phosphohydrolase. This enzyme participates in pantothenate and coa biosynthesis.