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The mammalian D-amino acid oxidase (DAO) and Daspartate oxidase (DDO) are presumed to regulate the levels of several endogenous and exogenous D-amino acids in various organs; however, their physiological roles in vivo remain to be fully clarified. The oxidation reactivity of DAO and DDO was quantitatively analyzed in silico. The stereo structure of mammalian DAO was constructed in silico from pig kidney DAO (PDB ID: 1VE9) and optimized using the MM2 calculation, then, atomic partial charge (apc) of key atoms was calculated using a MOPAC-PM5 program, and the specific activity (U mg protein) for several substrate amino acids was correlated with the change of apc values (apc) of -carbon (C) of the amino acids. The feasibility of the constructed mammalian DAO was analyzed by the comparison with four downloaded mammalian DAOs. Furthermore, the stereo structures of mouse DDO was constructed in silico from pig DAO and optimized using MM2 calculation, and apc of key atoms was calculated using MOPAC-PM5 program, and then correlated with the oxidation reactivity. Likewise, the DDO mutants carrying a substitution of alanine, glycine, or tyrosine for the active site residue serine-308 (S308A, S308G, and S308Y mutant, respectively) and a double-point substitution of glycine and tyrosine for serine-308 and glycine-309, respectively (S308G-G309Y mutant), were also analyzed. Correlation coefficient between the specific activity (U mg protein) of the constructed mammalian DAO, downloaded mammalian DAO (PDB ID: 2du8, 3g3e, and 3znn) and apc of C of substrate was over 0.8 (n = 14). Furthermore, the reactivity (Vmax/ Km) of mouse DDO and DDO mutants was correlated with apc of C and N of D-aspartic acid with r = 0.849 (n = 5) and r = 0.876 (n = 5), and with that of those of NMDA with r = 0.902 (n = 5) and r = 0.741 Quantitative in silico analysis of selective enzyme reaction of mammalian D-amino acid oxidase and acidic D-amino acid oxidase mutants SDRP Journal of Computational Chemistry & Molecular Modelling (ISSN: 2473-6260) DOI:10.25177/JCCMM.2.3.2 Research