D-amino acid oxidase (DAAO, DAO, EC 220.127.116.11) is a typical flavin protease with flavin adenine (FAD) as its auxiliary group, which oxidizes the amino group of D-amino acid to produce corresponding ketoacids and ammonia. The catalytic reactions are as follows:
D-amino acid+O 2_ketonic acid+H 2+NH 3
D-amino acid oxidase combines with coenzyme FAD, which reacts with D-amino acid. D-amino acid dehydrogenation becomes the corresponding sub-amino acid and combines with reducing FAD. This step is the only enzymatic reaction in the whole reaction. In the presence of molecular oxygen, reductive FAD is oxidized again and converted into hydrogen peroxide; amino acid hydrolysis into A-ketonic acid and ammonia, but in vivo. In the presence of hydrogen peroxide, A-ketonic acid decarboxylates to produce corresponding acids.
D-amino acid oxidase has high stereoisomeric selectivity and broad spectrum for catalytic reaction substrates. It can be widely used in qualitative and quantitative analysis of D-amino acid, biosensor, production of L-amino acid and A-ketonic acid.
Preservation buffer: Tris buffer, pH 8.0
Source: Gene recombinant expression
Molecular weight: about 41 kDa (SDS-PAGE detection)
Purity: > 90% (SDS-PAGE test)
Preservation Conditions: 4 C or - 20 C long-term preservation to avoid repeated freezing and thawing
Transportation Conditions: Low Temperature Ice Bag
Safety Tips: Not Used in Human Experiments
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