Literature summary for 1.4.3.3 extracted from

Padhi, A.; Zhang, K.
Mechanistic insights into the loss-of-function mechanisms of rare human D-amino acid oxidase variants implicated in amyotrophic lateral sclerosis (2020), Sci. Rep., 10, 17146 .

Search for more literature for 1.4.3.3

Application

Application	Comment	Organism
medicine	comprehensive analysis of catalogued DAAO rare variants triggering amyotrophic lateral sclerosis. Certain rare variants disrupt key interactions with the active site and decrease the conformational flexibility of active site loop comprising residues 216-228, which is essential for substrate binding and product release. These variants lost crucial interactions with the cofactor flavin-adenine-dinucleotide, resulting in weaker binding affinity	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	DAO variants including V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E significantly reduce fluctuations around the active site loop residues and close to the hydrophobic stretch region of residues 47-51. In molecular dynamics simulations, V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E variants exhibit nearly similar radius of gyration, the H78Y, R279Q and S340F variants including the wild-type exhibit a slightly increased profile. Variants V5A, D46N, F90V, P103L, R115W, P119L, L215F, P268S, R283Q, R286C, L329F and G331E experience more compact structure than wild-type and H78Y, R279Q and S340F during the course of simulations	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P14920	-	-

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Release 2023.1 (January 2023)