Sulfite oxidase Mo centre domain (EC 1.8.3.1), Homo sapiens

Sulfite oxidase (EC 1.8.3.1) is a homodimeric protein localized in the intermembrane space of mitochondria of all eukaryotic organisms. Each subunit contains an N-terminal domain, with a heme cofactor, and a C-terminal domain, with a molybdopterin cofactor (MoVI). The enzyme catalyzes the oxidation of sulfite to sulfate, which takes place at the molybdenum centre, and is the final reaction in the oxidative degradation of the sulfur amino acids cysteine and methionine. Sulfite oxidase deficiency results in neurological abnormalities which are often fatal at an early age. NZYTech`s sulfite oxidase comprises the recombinant molybdenum C-terminal domain of Homo sapiens. The enzyme is provided in 3.2 M ammonium sulphate. The enzyme specific activity, at 25 °C, is 0.5 U/mg (measured at pH 8.5, using sulfite as substrate at saturation concentrations). The enzyme exhibits an activity of around 100 units/mg of protein using ferricyanide as electron acceptor, as described by Temple et al. (2000, see below). Activity: 1.0 U/ml Temperature and pH optimum/stability: The optimum pH and temperature are 8.5 and 25°C, respectively. Shipping Conditions: Room Temperature. Storage Conditions: 2 °C to 8 °C. Features: >95% pure (SDS-PAGE). SUOX, EC=1.8.3.1, Sulfite oxidase, mitochondrial