Diamine Oxidase from porcine kidney

Diamine oxidase from porcine kidney is a homodimer consisting of two equal subunits with a molecular weight of 87 kDa each. Each subunit contains one molecule of pyridoxal phosphate and one atom of copper. The molecular mass of the enzyme is found to be 170 kDa. The enzyme is a glycoprotein containing 5% hexose, 3.3% glucosamine, 2.6% N-acetylglucosamine, and 0.25% N-acetylneuraminic acid. The enzyme exhibits a high affinity for concanavalin A. Optimum pH with cadverine and histamine as substrates is found to be 6.3-7.4.

Diamine Oxidase from porcine kidney has been used in the construction of histamine biosensor.

Diamine oxidase from porcine kidney has been used in a study to investigate a luminescence-based test for determining ornithine decarboxylase activity. Diamine oxidase from porcine kidney has also been used in a study to investigate N-linked oligosaccharide structures in diamine oxidase.

Diamine Oxidase catalyzes the oxidation of monoamines, diamines, and histamine to aldehydes, ammonia, and hydrogen peroxide. The enzyme is classified as a copper amine oxidase and it is a key enzyme in nitrogen metabolism. Diamine oxidase is inhibited by diethyldithiocarbamate, phenylhydrazine, semicarbazide, cyanide, isonicotinic acid hydrazide.

One unit will oxidize 1.0 μmole of putrescine per hr at pH 7.2 at 37 °C.