A NON-SPECIFIC ADENINE NUCLEOTIDE DEAMINASE FROM DESULFOVIBRIO DESULFURICANS

1. 1. A non-specific adenine nucleotide deaminase, which is equally active with AMP, ADP or AtP, was extracted from Desulfovibrio desulfuricans, strain Berre S, and purified approx. 800-fold. 2. 2. Enzyme preparations contained 4% of nucleic acids, which stabilised the activity during storage. 3. 3. The enzyme was competitively inhibited by various substances with the following values for Ki: urea (410 mM), p-mercuribenzoate (11.8 μM), HgCl2 (5.3 μM), CuSO4 (67 μM) and the anions, β,β dimethyl glutarate (3.2 mM), citrate (6.0 mM), succinate (18 mM), maleate (22 mM), phosphate (83 mM), cacodylate (134 mM) and Cl-. 4. 4. Low concentrations of F- and CN- caused non-competitive inhibition. © 1969.