磷酸二酯酶I 来源于东部菱背响尾蛇毒液

磷酸二酯酶 | 5'-核酸外切酶 | 寡核苷酸5'-核苷酸水解酶

5′-Exonuclease | Oligonucleate 5′-nucleotidohydrolase

P128636-100UN

100U

EnzymoPure™

≥20 units/mg dry weight

Venom exonuclease (Phosphodiesterase I) successively hydrolyzes 5'-mononucleotides from 3'-OH-terminated ribo- and deoxyribo-oligonucleotides. The enzyme has an optimal pH range of 9.8-10.4 and a molecular weight of 115 kDa. Phosphodiesterase is inhibited by reducing agents such as glutathione, cysteine and ascorbic acids. It is completely inhibited by 5mM EDTA while ATP, ADP and AMP are partial inhibitors. The enzyme has an absolute requirement for Mg2+.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. Molecular weight: 115,000 (Philipps 1975). Composition: A glycoprotein which binds concanavalin A. (Sulkowski and Laskowski 1961). Optimum pH: 9.8-10.4 (Philipps 1975). Inhibitors: Reducing agents such as glutathione, cysteine and ascorbic acid (Razell 1963). It is completely inhibited by 5 mM EDTA while ATP, ADP and AMP are partial inhibitors. Activators: The enzyme has an absolute requirement for Mg2+; Philipps (1975) indicates an optimum concentration of 15 mM. Specificity: The enzyme has been purified by Dolapchiev et al. (1974) and Sulkowski and Laskowski, Sr. (1961) with endonuclease activity being eliminated as well as 5'-nucleotidase and nonspecific monophosphatase. It is nonspecific with respect to base or sugar moieties of nucleotides. A variety of synthetic substrates are hydrolyzed. See review by Razell (1963). Ogilvie and Hruska (1976) indicate that exonuclease will not recognize nucleoside units in the syn conformation. See also Philipps and Chiemprasert (1975). ADP-ribosylated proteins are cleaved at the pyrophosphate linkages by venom phosphodiesterase to yield phosphoribosyl-AMP (Hayaishi 1976).

磷酸二酯酶 I 能断裂磷酸二酯键，并催化各种核苷酸多聚磷酸盐的水解。磷酸二酯酶 I 通过磷脂酰肌醇特异性磷脂酶 C 从真核细胞质膜中释放出来。