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Exploring the Dynamics of D‐Amino Acid Oxidase Using Molecular Dynamics Simulations
Author(s) -
Jonsson Amanda L,
Kueffer Lauren,
Birdsong Garrick
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.462.3
Subject(s) - oxidative deamination , d amino acid oxidase , amino acid , oxidase test , molecular dynamics , biochemistry , chemistry , enzyme , serine , stereochemistry , computational chemistry
The D‐amino acid oxidase (DAAO) enzyme catalyzes the oxidative deamination of D‐amino acids to give ammonia and an α‐keto acid, coupled to the reduction of the cofactor FAD. In humans DAAO plays a key role in modulating the degradation pathway of the important signaling molecule D‐serine in the brain. We ran all‐atom, explicit‐solvent molecular dynamics simulations of the wild‐type human DAAO, several mutations known to increase DAAO activity or FAD binding (D31H, R279A, and W209R), and mutations known to decrease activity or binding (R199Q and R199W). Theses mutations are spread throughout the protein structure, some far from the FAD‐binding site and active site. We aim to better understand how small changes in the sequence can lead to changes in overall activity and binding affinity. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .