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Serine 335 at the active site of d-amino acid oxidase from the yeast Rhodotorula gracilis (RgDAAO) is not conserved in other DAAO sequences. To assess its role in catalysis, it was mutated to Gly, the residue present in mammalian DAAO, an enzyme with a 35-fold lower turnover number with d-alanine. The spectral and ligand binding properties of the S335G mutant are similar to those of wild-type enzyme,...
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