Phosphodiesterase I successively hydrolyzes 5'-mononucleotides from 3'-hydroxy-terminated ribo- and deoxyribo-oligonucleotides. ADP-ribosylated proteins are cleaved at the pyrophosphate linkages by venom phosphodiesterases to yield phosphoribosyl-AMP.
- Enzyme that is used to break phosphodiester bonds
- Membrane-bound glycoprotein
- Catalyze the hydrolysis of various nucleotide polyphosphates
Phosphodiesterase I is used in phosphodiesterase activation assays to hydrolyze AMP. The enzyme has been widely utilized as a tool for structural and sequence studies of nucleic acids.
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.
Specific Activity: ≥20 µ/mg solid
Key Applications: Tool for structural and sequence studies of nucleic acids, Phosphodiesterase activation assay
Application Areas: Molecular biology
Product Type: Proteins, Enzymes & Peptides
Presentation: Lyophilzed Powder
Format: Powder
pH: Optimum pH=9.8 to 10.4.5(Lit.)
NOTES: Activators: The enzyme has an absolute requirement for Mg2+; Philipps indicates an optimum concentration of 15 mM. Inhibitors: Reducing agents such as gluctathione, cysteine and ascorbic acid. It is completely inhibited by 5 mM EDTA while ATP, ADP and AMP are partial inhibitors. Composition: A glycoprotein which binds concanavalin A.
Storage & Handling: Store at -20 °C.