嗜热真菌 Rasamsonia emersonii 菌株 YA 中一种独特的 D-氨基酸氧化酶的 X 射线结构分析。
X-ray structure analysis of a unique D-amino-acid oxidase from the thermophilic fungus Rasamsonia emersonii strain YA.
机构信息
Department of Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan.
Department of Biomolecular Science, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.
出版信息
Acta Crystallogr F Struct Biol Commun. 2020 Nov 1;76(Pt 11):517-523. doi: 10.1107/S2053230X20013333. Epub 2020 Oct 23.
D-Amino-acid oxidases (DAAOs) catalyze the oxidative deamination of neutral and basic D-amino acids. The DAAO from the thermophilic fungus Rasamsonia emersonii strain YA (ReDAAO) has a high thermal stability and a unique broad substrate specificity that includes the acidic D-amino acid D-Glu as well as various neutral and basic D-amino acids. In this study, ReDAAO was crystallized by the hanging-drop vapor-diffusion method and its crystal structure was determined at a resolution of 2.00 Å. The crystal structure of the enzyme revealed that unlike other DAAOs, ReDAAO forms a homotetramer and contains an intramolecular disulfide bond (Cys230-Cys285), suggesting that this disulfide bond is involved in the higher thermal stability of ReDAAO. Moreover, the structure of the active site and its vicinity in ReDAAO indicates that Arg97, Lys99, Lys114 and Ser231 are candidates for recognizing the side chain of D-Glu.
D-氨基酸氧化酶（DAAO）催化中性和碱性 D-氨基酸的氧化脱氨。耐热真菌 Rasamsonia emersonii 菌株 YA 的 DAAO（ReDAAO）具有较高的热稳定性和独特的广泛底物特异性，包括酸性 D-氨基酸 D-Glu 以及各种中性和碱性 D-氨基酸。在本研究中，ReDAAO 通过悬滴气相扩散法进行结晶，并在 2.00 Å 的分辨率下确定了其晶体结构。酶的晶体结构表明，与其他 DAAO 不同，ReDAAO 形成同源四聚体并包含一个分子内二硫键（Cys230-Cys285），表明该二硫键参与了 ReDAAO 的更高热稳定性。此外，ReDAAO 活性位点及其附近的结构表明，Arg97、Lys99、Lys114 和 Ser231 是识别 D-Glu 侧链的候选者。
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