Literature summary for 1.4.3.3 extracted from

Padhi, A.; Hazra, S.
Insights into the role of D-amino acid oxidase mutations in amyotrophic lateral sclerosis (2019), J. Cell. Biochem., 120, 2180-2197 .

Search for more literature for 1.4.3.3

Application

Application	Comment	Organism
medicine	molecular dynamics simulations of wild-type, and all reported amyotrophic lateral sclerosis-associated DAO mutants. The mutations disrupt several key interactions with the active site residues and decrease the conformational flexibility of active site loop comprising 216 to 228 residues, necessary for substrate binding and product release, mainly due to the distortion of critical salt bridge and hydrogen bond interactions compared with wild-type. DAO mutants have a lower binding affinity toward cofactor flavin adenine dinucleotide and substrate iminoserine than the wildtype	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular modeling of active site loop of wild-type and amyotrophic lateral sclerosis?associated DAO mutants such as R199W, R38H, R199Q, and Q201R	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P14920	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)