抄録
1. A method was described for the purification of ATP deaminase [ATP aminohydrolase, EC class 3. 5.4] from wheat-bran koji of Microsporum audouini.
2. This enzyme was found to deaminate adenosine tetraphosphate, ADP, 5'-AMP, ADP-ribose, ADP-glucose, dATP, dADP, dAMP, 3', 5'-cyclic AMP, NAD, FAD, CoA, and adenosine, as well as ATP. Adenine, 2'-AMP, and NADP were not attacked by this enzyme.
3. The deaminated product of ATP was proved to be ITP.
4. The stoichiometry and equilibrium of deamination were studied.
5. The activation energy of the enzyme activity was found to be approximately 7, 300 calories.
6. The optimal pH was 5.0 in acetate buffer.
7. The Michaelis-Menten constant was calculated to be 4×l0-5M at 30°C.
