A5222
D-Amino Acid Oxidase from porcine kidney
powder, ≥1.5 units/mg solid
Synonym(s):
D-AAO, D-Amino acid: oxygen oxidoreductase (deaminating)
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About This Item
Recommended Products
form
powder
specific activity
≥1.5 units/mg solid
storage temp.
−20°C
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Application
D-amino acid oxidase (DAO) is a potential target molecule for the treatment of chronic pain and schizophrenia . D-amino acid oxidase is used to oxidize D-amino acids to their corresponding imino acids.
Unit Definition
One unit will oxidatively deaminate 1.0 μmole of D-alanine to pyruvate per minute at pH 8.3 at 25 °C, in the presence of a catalase.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Glutamine 89 is a key residue in the allosteric modulation of human serine racemase activity by ATP.
Andrea V Canosa et al.
Scientific reports, 8(1), 9016-9016 (2018-06-15)
Serine racemase (SR) catalyses two reactions: the reversible racemisation of L-serine and the irreversible dehydration of L- and D-serine to pyruvate and ammonia. SRs are evolutionarily related to serine dehydratases (SDH) and degradative threonine deaminases (TdcB). Most SRs and TdcBs
Pamela Cappelletti et al.
The FEBS journal, 281(3), 708-723 (2013-11-19)
Human D-amino acid oxidase (EC 1.4.3.3; hDAAO) is a peroxisomal flavoenzyme significantly enriched in the mammalian brain. hDAAO has been proposed to play (with serine racemase; EC 5.1.1.18) an essential role in the catabolism of D-serine, an 'atypical' key signalling
Seth C Hopkins et al.
The Journal of pharmacology and experimental therapeutics, 345(3), 502-511 (2013-03-23)
Inhibition of d-amino acid oxidase (DAAO) activity is a potential target for the treatment of chronic pain. Here we characterized the effects of systemic administration of the DAAO inhibitor 4H-furo[3,2-b]pyrrole-5-carboxylic acid (SUN) in rat models of neuropathic and inflammatory pain.
Makoto Yoshimoto et al.
Enzyme and microbial technology, 52(1), 13-19 (2012-12-04)
Oligolamellar phospholipid vesicles incorporated with d-amino acid oxidase from porcine kidney (OV-DAO) were prepared by encapsulating pre-formed enzyme-bound unilamellar vesicles (UV-DAO) with bilayers of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC). The bilayer of UV-DAO was composed of POPC, 30 mol% of cholesterol and 15
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