D-Amino Acid Oxidase, Porcine Kidney (D-AAO, D-Amino acid: oxygen oxidoreductase, deaminating, DAO, OXDA)

D-Amino Acid Oxidase is a flavoprotein oxidase, flavin being the only prosthetic group. The enzyme from porcine kidney has been extensively studied. It is isolated as a stable crystalline complex with benzoate, from which the holo and apoenzyme may be prepared. The benzoate is readily exchanged for a substrate.\n\nD-Amino acid oxidase catalyzes the oxidation of D-amino acids as shown below:\n D-AAO \nRCHNH2COOH + O2 + H2O ------> RCOCOOH + NH3 + H2O2 \nThe D isomers of alanine, methionine, valine, isoleucine, phenylalanine and proline serve as good substrates while the L isomers do not react.\n\nD-Amino acid oxidase has several possible applications such as the determination of D-amino acids, the separation of natural L- amino acid isomers from a racemic mixture and in the preparation of keto acids. The usefulness and application of D-amino acid oxidase can be significantly increased if it is available in an immobilized form (Parkin, K. and Hultin, H.O., Biotech. and Bioeng., Vol XXI, 939, 1979).\n\nEnzyme Commission (EC) Number: 1.4.3.3 (BRENDA | IUBMB )\nMDL number: MFCD00081546\nEG/EC Number: 232-563-5\n\nSource:\nPorcine kidney\n\nForm:\nSupplied as a chromatographically purified, lyophilized powder.\n\nProtein: 10 mg/ml (biuret) \n\nActivity:\n~10-20U/mg Protein\n\nMolecular Weight:\nMonomeric, 38,000-39,000 D\n\nUnit Definition:\nThe amount of enzyme that will deaminate by oxidation one micromole of D-alanine to pyruvate per minute at pH 8.3, at 37 degrees C in the presence of catalase.\n\nThe assay is based on the method described by Bergmeyer (Methods of Enzymatic Analysis, Bergmeyer, H.U. ed. Vol 1, 431, 1974, Academic Press, New York). The decrease in the absorbance at 340nm, due to the oxidation of NADH, is a measure of D-amino acid oxidase activity.\n\nQuality Control:\nSDS-PAGE\n\nUnit Definition: One unit will oxidatively deaminate 1umole of D-alanine to pyruvate per minute at pH 8.3 at 25 degrees C, in the presence of a catalase.\n\nStorage and Stability:\n6 months at -20 degrees C

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SPECIFICATIONS

Catalog Number

A1373-01

Size

100U

References

1. Bright, H., and Porter, D.: in The Enzymes, XII, Pt. B, 3rd ed., (Boyer, P., ed.), Academic Press, NY, 445 (1975). 2. Curti, B., Ronchi, S., Branzoli, U., Ferri, G., and Williams, C.: Improved Purification, Amino Acid Analysis and Molecular Weight of Homogeneous D-Amino Acid Oxidase from Pig Kidney, Biochim. Biophys. Acta, 327, 266 (1973). 3. Dixon, M., and Kleppe, K.: D-Amino Acid Oxidase. I. Dissociation and Recombination of the Holoenzyme, Biochim. Biophys. Acta, 96, 357 (1965a). 4. Tu, S., and McCormick, D.: Photoinactivation of Porcine D-Amino Acid Oxidase with Flavin Adenine Dinucleotide, J. Biol. Chem., 248, 6339 (1973). 5. Tu, S., Edelstein, S., and McCormick, D.: A Modified Purification Method and Properties of Pure Porcine D-Amino Acid Oxidase, Arch. Biochem. Biophys., 159, 889 (1973). 6. Yagi, K., and Natsume, K.: Inhibitory Action of Pyruvate on D-Amino Acid Oxidase, J. Biochem. Japan, 55, 529 (1964). 7. Yagi, K., and Okamura, K.: Isolation by Crystallization of Fully Reduced D-Amino Acid Oxidase, Biochem. Biophys. Res. Comm., 21, 399 (1965a).

Alternative Names

EC=1.4.3.3; Porcine Kidney