Spectroscopic and enzymic features of yeast peroxisomal catalase

In the enzymic group of oxidoreductases the key position occupies the enzym e catalase(1.11.1.6) which can not only reduce but also oxidize a molecule of hydrogen peroxide yielding molecular oxygen and water. The scope of this paper is to give an overview of the occurrence and the properties of the a bundant enzyme catalase which is essential for all organisms with aerobic m etabolism and defends living cell against toxic oxygen derivatives resultin g in the metabolism. The enzymic properties of the three subgroups of the c atalase family, ie. true catalases, catalase-peroxidases and non-heme catal ases are discussed. The paper further concentrates on affinity-purified cat alase A from the yeast Saccharomyces cerevvisiae the properties of which ar e compared with those found in the literature. The experiments presenting t he stability and heme content of catalase A from the above yeast are report ed. Observed data together with enzymic properties and structural features support the classification of yeast catalase A as a true - or typical catal ase.