Role of the active site residues arginine-216 and arginine-237 in the substrate specificity of mammalian d-aspartate oxidase
…, K Maeda, T Hanai, M Sekine, T Furuchi, H Homma
Index: Katane, Masumi; Saitoh, Yasuaki; Maeda, Kazuhiro; Hanai, Toshihiko; Sekine, Masae; Furuchi, Takemitsu; Homma, Hiroshi Amino Acids, 2011 , vol. 40, # 2 p. 467 - 476
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Citation Number: 8
Abstract
Abstract d-Aspartate oxidase (DDO) and d-amino acid oxidase (DAO) are flavin adenine dinucleotide-containing flavoproteins that catalyze the oxidative deamination of d-amino acids. Unlike DAO, which acts on several neutral and basic d-amino acids, DDO is highly specific for acidic d-amino acids. Based on molecular modeling and simulated annealing docking analyses, a recombinant mouse DDO carrying two substitutions (Arg-216 to Leu ...
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