Catalase is ubiquitously found in animals, plants, fungi, and humans. It is made up of looped polypeptide chains that are arranged as tetramers or dimers and a core, that contains iron or manganese ions. Catalase can be differentiated into two types such as heme-containing (type I), which possesses an iron-porphyrin cofactor and a non-heme-containing (type II), which possesses a dinuclear manganese active site.
Catalase from Corynebacterium glutamicum has been used to identify and characterize purified bacterial peptide (PPBP) produced from Bacillus thuringiensis. It has also been used to study its inhibition by nitric oxide.
Catalase is an antioxidant enzyme that plays a role in alleviating oxidative stress by the removal of hydrogen peroxide to produce oxygen and water. Lower levels of catalase lead to several age-related disorders including hypertension, anemia, vitiligo, Parkinson′s disease, Alzheimer′s disease, schizophrenia, bipolar disorders, diabetes mellitus, and cancer.
1 U corresponds to the amount of enzyme which decomposes 1 μmol H2O2 per minute at pH 7.0 and 25°C
contains ~30% glycerol, 10% ethanol