DAAO Human, Active
D-Amino Acid Oxidase 2, D-Amino-Acid Oxidase, EC 1.4.3.3, DAMOX, DAAO, EC 1.4.3, OXDA.
Greater than 95.0% as determined by SDS-PAGE.
Description
DAAO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (1-347) and having a molecular mass of 41.6 kDa. DAAO Humanis fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
D-amino-acid oxidase, also known as DAAO, is an enzyme that catalyzes the oxidative deamination of D-amino acids. This process uses FAD (flavin adenine dinucleotide) as a cofactor and produces alpha-keto acids, ammonia, and hydrogen peroxide. DAAO is believed to play a role in maintaining acid-base balance in kidney tissue and detoxifying byproducts of D-amino acid breakdown, which can accumulate during cellular aging.
Recombinant human DAAO, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 367 amino acids (residues 1-347), with a molecular weight of 41.6 kDa. This DAAO protein includes an N-terminal His-tag of 20 amino acids. Purification is achieved using proprietary chromatographic techniques.
The formulation for DAAO Human protein (0.5mg/ml) consists of 20mM Tris-HCl buffer at pH 8.0, 20% glycerol, and 1mM DTT.
The purity is determined to be greater than 95.0% based on SDS-PAGE analysis.
The specific activity is measured to be greater than 3.5 units/mg. One unit is defined as the amount of enzyme required to oxidatively deaminate 1.0 µmol of D-alanine to pyruvate per minute at a pH of 8.5 and temperature of 37°C in the presence of catalase.
D-Amino Acid Oxidase 2, D-Amino-Acid Oxidase, EC 1.4.3.3, DAMOX, DAAO, EC 1.4.3, OXDA.
MGSSHHHHHH SSGLVPRGSH MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG LWQPYLSDPN NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE AIPDPSWKDT VLGFRKLTPR ELDMFPDYGY GWFHTSLILE GKNYLQWLTE RLTERGVKFF QRKVESFEEV AREGADVIVN CTGVWAGALQ RDPLLQPGRG QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG IFQLGNWSEL NNIQDHNTIW EGCCRLEPTL KNARIIGERT GFRPVRPQIR LEREQLRTGP SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL.
Product Science Overview
D-Amino Acid Oxidase (DAAO) is a flavin adenine dinucleotide (FAD)-dependent oxidase that catalyzes the oxidative deamination of D-amino acids into their corresponding imino acids, which subsequently hydrolyze to produce α-keto acids and ammonia . This enzyme is highly specific for D-amino acids, excluding the acidic ones .
DAAO was first discovered in pig kidney in 1935 by Krebs . Since then, it has been extensively studied as a prototype of FAD-dependent oxidases. The enzyme’s structure is highly conserved across different species, with minor variations that account for functional differences between microbial and human DAAO .
Human DAAO is an FAD-containing flavoenzyme that plays a crucial role in the central nervous system by degrading the neuromodulator D-serine . D-serine acts as a co-agonist of N-methyl D-aspartate (NMDA) receptors, which are involved in various brain functions and pathological conditions . The enzyme’s activity is finely regulated to maintain appropriate D-serine levels in the brain .
DAAO catalyzes the oxidative deamination of neutral D-amino acids, resulting in the formation of imino acids, which spontaneously hydrolyze to α-keto acids and ammonia . The reoxidation of FADH2 by molecular oxygen generates hydrogen peroxide as a byproduct . This reaction is of significant biotechnological relevance, with applications in biocatalysis, biosensors, and cancer therapy .
- Biocatalysis: DAAO is used to produce α-keto acids from D-amino acids and to resolve racemic mixtures of amino acids .
- Biosensors: The enzyme is employed in biosensors for detecting D-amino acids .
- Cancer Therapy: DAAO has potential applications in cancer therapy due to its ability to generate hydrogen peroxide, which can induce oxidative stress in cancer cells .
Human DAAO interacts with various proteins that modulate its activity, targeting, and stability within cells . The enzyme’s activity is also influenced by the binding of active-site ligands and substrates, which stabilize flavin binding and enhance catalytic competence . Current research focuses on the epigenetic modulation of DAAO expression and the role of post-translational modifications in regulating its biochemical properties .
