D-aspartate Oxidase
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D-aspartate Oxidase
In enzymology, a D-aspartate oxidase () is an enzyme that catalyzes the chemical reaction :D-aspartate + H2O + O2 \rightleftharpoons oxaloacetate + NH3 + H2O2 The 3 substrates of this enzyme are D-aspartate, H2O, and O2, whereas its 3 products are oxaloacetate, NH3, and H2O2. This enzyme belongs to the FAD dependent oxidoreductase family, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is D-aspartate:oxygen oxidoreductase (deaminating). Other names in common use include aspartic oxidase, and D-aspartic oxidase. This enzyme participates in alanine and aspartate metabolism. It employs one cofactor, FAD. The enzyme is encoded by DDO gene. See also * DAO * Diamine oxidase * D-amino acid oxidase D-amino acid oxidase (DAAO; also OXDA, DAMOX) is an enzyme with the function on a molecular level to oxidize D-amino acids to the corresponding α-keto acids, producing ammonia and hydrogen peroxide. ...
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Enzymology
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ...
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