Purification and Properties of Hog Liver Nicotinamide Deamidase
1982 Volume 56 Issue 12 Pages 659-664
Details
1982 Volume 56 Issue 12 Pages 659-664
Nicotinamide deamidase (EC 3.5.1.19) was partially purified from hog liver acetone powder and properties of this enzyme were investigated. Molecular weight of this enzyme was estimated as 180,000 daltons. The enzyme was stable at pH between 6 and 8. The optimum pH of the enzyme reaction was found at 6.8. The K_m value was 0.126 M. This enzyme reaction was inhibited by p-chloromercuribenzoate, Fe^<3+>, Hg^<2+>, Al^<3+> and Co^<2+>. NAD, NADH and N^1_methylnicotinamide were also inhibitory. This enzyme reaction was found to be irreversible. These properties were compared with those of enzymes found in various species, and a possible function of the enzyme in NAD biosynthesis and metabolism was discussed.
