Literature summary for 1.4.3.1 extracted from

Katane, M.; Kanazawa, R.; Kobayashi, R.; Oishi, M.; Nakayama, K.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Homma, H.
Structure-function relationships in human D-aspartate oxidase characterisation of variants corresponding to known single nucleotide polymorphisms (2017), Biochim. Biophys. Acta, 1865, 1129-1140 .

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Protein Variants

Protein Variants	Comment	Organism
R216Q	single nucleotiode polymorphism, reduces enzyme activity towards acidic D-amino acids, decreases the binding affinity for the coenzyme FAD and decreases the temperature stability. Cultured mammalian cells reveal elevated D-aspartate level in cultures of R216Q cells	Homo sapiens
S308N	single nucleotiode polymorphism, reduces enzyme activity towards acidic D-amino acids, decreases the binding affinity for the coenzyme FAD and decreases the temperature stability. Cultured mammalian cells reveal elevated D-aspartate level in cultures of R216Q cells	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	C9K4X7	-	-

Synonyms

Synonyms	Comment	Organism
DDO	-	Homo sapiens

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Release 2023.1 (January 2023)