Properties and applications of immobilized snake venom NAD glycohydrolase.
The NAD glycohydrolase (NADase) from Bungarus fasciatus snake venom was adsorbed on concanavalin A-Sepharose, and demonstrated to retain both hydrolase and transglycosidase activities in the bound form. The matrix-bound enzyme was stable to repeated washing with buffer and storage at 4 degrees C. The bound enzyme exhibited the same Km value for hydrolysis of nicotinamide-1,N6-ethenoadenine dinucleotide as previously measured with the soluble, purified form of the enzyme. The bound NADase was used repeatedly for a preparative-scale synthesis of 3-acetylpyridine adenine dinucleotide. It was further demonstrated that the immobilized enzyme could be prepared directly from crude snake venom, thus avoiding the time required for purification. The application of the immobilized snake venom NADase for the preparation of pyridine nucleotide coenzyme analogs has many advantages over procedures used previously for analog synthesis.
D002384:Catalysis; D004546:Elapid Venoms / Q000032:analysis*; D004800:Enzymes, Immobilized; D006868:Hydrolysis; D009699:N-Glycosyl Hydrolases / Q000378:metabolism*; D009244:NAD+ Nucleosidase; D012685:Sepharose / Q000031:analogs & derivatives
D004546:Elapid Venoms; D004800:Enzymes, Immobilized; C028326:concanavalin A-sepharose; D012685:Sepharose; D009699:N-Glycosyl Hydrolases; D009244:NAD+ Nucleosidase