Human D-Amino Acid Oxidase: Structure, Function, and Regulation
نویسندگان
چکیده
منابع مشابه
Competitive Inhibitors Unveil Structure/Function Relationships in Human D-Amino Acid Oxidase
D-amino acid oxidase (DAAO) catalyzes the oxidative deamination of several neutral D-amino acids and is the enzyme mainly responsible (together with serine racemase) for degrading D-serine (D-Ser) in the central nervous system of mammals. This D-amino acid, which binds the coagonist site of the N-methyl-D-aspartate receptor, is thus a key neuromodulator of glutamatergic neurotransmission. Alter...
متن کاملBiological role of D-amino acid oxidase and D-aspartate oxidase. Effects of D-amino acids.
D-Amino acids administered to animals are absorbed by the intestine and transported through the blood-stream to solid tissues where they are oxidized in vivo by D-amino acid oxidase and D-aspartate oxidase to produce the same compounds they do in vitro; i.e. NH3, H2O2, and the keto acid corresponding to the amino acid ingested. In the liver and kidneys of the animals, an inverse relationship ex...
متن کاملD-Amino Acid Oxidase and Metagenomics
D-amino acid oxidase (DAAO, EC 1. 4. 3. 3) converts D-amino acid to a corresponding α-keto acid via deamination. D-amino acid oxidase is one of the most important enzymes responsible for maintenance proper level of D-amino acids, which play a key role in regulation of many processes in living cells. This paper summary the applications of D-amino acid oxidase in agricultural and industry practic...
متن کاملBiochemical Properties of Human D-Amino Acid Oxidase
D-amino acid oxidase catalyzes the oxidative deamination of D-amino acids. In the brain, the NMDA receptor coagonist D-serine has been proposed as its physiological substrate. In order to shed light on the mechanisms regulating D-serine concentration at the cellular level, we biochemically characterized human DAAO (hDAAO) in greater depth. In addition to clarify the physical-chemical properties...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Frontiers in Molecular Biosciences
سال: 2018
ISSN: 2296-889X
DOI: 10.3389/fmolb.2018.00107