Catalase

9001-05-2

1000

10 mM in DMSO

Metabolic Enzyme/Protease; NF-kappaB; Immunology/Inflammation

Catalase is a key enzyme in the metabolism of H₂O₂ and reactive oxygen species (ROS), and its expression and localization is markedly altered in tumors^[1]. Free oxygen radical scavenger. In Vitro: Catalase, the enzyme that metabolizes H₂O₂ but also reacts with a multitude of other substrates. The active site of catalase contains an iron atom. Human catalase contains four identical subunits, each subunit containing four distinct domains and one prosthetic heme group. The four domains include: (1) a N-terminal arm which contains a distal histidine, an essential amino acid for the catalase reaction; (2) a beta-barrel domain that contains eight beta-barrels arranged in an antiparallel fashion with six alpha-helical insertions, conferring the hydrophobic core of the protein necessary for the tri-dimensional structure of the enzyme; (3) a connection domain which contains the tyrosine residue that binds the heme group; and finally (4) an alpha-helical domains, which is important for NADPH binding^[1].