Momoi K, Fukui K, Watanabe F, Miyake Y
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka, Japan.
FEBS Lett. 1988 Sep 26;238(1):180-4. doi: 10.1016/0014-5793(88)80252-7.
cDNA clones encoding D-amino acid oxidase were isolated from a human kidney cDNA library by hybridization with cDNA for the pig enzyme. The cDNA insert of 2.0 kilobase pairs long provided coding information for a protein consisting of 347 amino acids. The molecular mass of the enzyme was calculated to be 39,410 Da. The amino acid sequence similarity between the pig and human enzymes is 84.4%, and among the active site residues proposed from chemical modification studies, methionine-110 of the pig enzyme was replaced by threonine. Northern blot analysis confirmed the expression of an mRNA of 2.0 kilobases encoding the D-amino acid oxidase in human kidney.
通过与猪D-氨基酸氧化酶的cDNA杂交，从人肾cDNA文库中分离出编码D-氨基酸氧化酶的cDNA克隆。长度为2.0千碱基对的cDNA插入片段提供了由347个氨基酸组成的蛋白质的编码信息。该酶的分子量经计算为39410道尔顿。猪和人酶之间的氨基酸序列相似性为84.4%，在化学修饰研究提出的活性位点残基中，猪酶的甲硫氨酸-110被苏氨酸取代。Northern印迹分析证实人肾中存在编码D-氨基酸氧化酶的2.0千碱基mRNA的表达。
