The food enzyme phosphodiesterase I (oligonucleotide 5′‐nucleotidohydrolase; EC 3.1.4.1) is produced with the non‐genetically modified Leptographium procerum strain FDA by DSM Food Specialties B.V. The food enzyme is free from viable cells of the production organism. It is intended to be used to process yeast and yeast products. Phosphodiesterase I exhibits phosphohydrolase activity against NAD, nucleoside diphosphate sugars, and nucleoside tniphosphates. The enzyme was first isolated from rattlesnake venom and has been the subject of several reviews. Razzell partially purified a mammalian PDE I from a porcine kidney, and subsequent cell fractionation studies by other workers demonstrated the enzyme in the plasma membrane of rat liver cells[1-2].
[1] D J Morley. “Distribution of phosphodiesterase I in normal human tissues.” Journal of Histochemistry & Cytochemistry 35 1 (1987): 75–82.
[2] on Food Contact Materials, EFSA Panel Enzymes and Processing Aids (CEP). “Safety evaluation of the food enzyme phosphodiesterase I from the non-genetically modified Leptographium procerum strain FDA.” EFSA Journal 22 4 (2024).
Phosphodiesterase (PDE) is any enzyme that is used to breaks phosphodiester bonds. It is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is used in phosphodiesterase activation assays to hydrolyze AMP. Product P3134 is from crude, dried Crotalus adamanteus venom.
Phosphodiesterase I breaks phosphodiester bonds and catalyzes the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is released from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C.
