来自可变三角酵母的对头孢菌素C具有高活性的D-氨基酸氧化酶的特性研究
Characterization of a D-amino acid oxidase with high activity against cephalosporin C from the yeast Trigonopsis variabilis.
作者信息
Szwajcer-Dey E, Miller J R, Kovacevic S, Mosbach K
机构信息
Pure and Applied Biochemistry, University of Lund, Sweden.
出版信息
Biochem Int. 1990;20(6):1169-78.
We describe an improved method to purify D-amino acid oxidase with activity towards cephalosporin C. The protein has a carbohydrate content of 1.3% and two molecules of non-covalently bound flavin cofactor per protein molecule. HPLC profiles and enzymatic analysis have indicated that the cofactor is FAD, even though fluorescence spectroscopy shows a slightly altered spectral profile in the 400-500 nm range compared to authentic FAD. N-terminal sequencing of the protein revealed a high level of similarity (56% identity in 25 amino acids) between the fungal and mammalian oxidase, and probably represents a "Rossman fold" with a beta-alpha-beta structure for the binding of the adenosyl moiety of the cofactor.
我们描述了一种改进的方法来纯化对头孢菌素C具有活性的D-氨基酸氧化酶。该蛋白质的碳水化合物含量为1.3%，每个蛋白质分子含有两个非共价结合的黄素辅因子分子。高效液相色谱（HPLC）图谱和酶学分析表明，该辅因子是黄素腺嘌呤二核苷酸（FAD），尽管荧光光谱显示，与纯FAD相比，在400 - 500纳米范围内其光谱轮廓略有改变。该蛋白质的N端测序显示，真菌和哺乳动物氧化酶之间具有高度相似性（25个氨基酸中有56%的同一性），并且可能代表一种具有β-α-β结构的“罗斯曼折叠”，用于结合辅因子的腺苷部分。
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