X-ray structure analysis of a unique d-amino-acid oxidase from the thermophilic fungus Rasamsonia emersonii strain YA

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.

Source: Acta Crystallographica Section F - October 23, 2020 Category: Biochemistry Authors: Shimekake, Y. Hirato, Y. Funabashi, R. Okazaki, S. Goto, M. Furuichi, T. Suzuki, H. Kera, Y. Takahashi, S. Tags: d-amino-acid oxidases flavoenzymes d-amino acids substrate specificity thermal stability thermophilic fungi Rasamsonia emersonii research communications Source Type: research