Acatalasemia

Acatalasemia is a rare hereditary deficiency of tissue catalase and is inherited as an autosomal recessive trait (03). This enzyme deficiency was discovered in 1948 by Takahara and Miyamoto (Tl). Two different types of acatalasemia can be distinguished clinically and biochemically. The severe form, Japanese-type acatalasemia, is characterized by nearly total loss of catalase activity in the red blood cells and is often associated with an ulcerating lesion of the oral cavity. The asymptomatic Swiss-type acatalasemia is characterized by residual catalase activity with aberrant biochemical properties. In four unrelated families with Japanese-type acatalasemia, a splicing mutation due to a G-to-A transition at the fifth nucleotide in intron 4 was elucidated (K20, W5). We have also determined a single base deletion resulting in the frameshift and premature translational termination in the Japanese patient (HI6). 

H16. Hirono, A., Sasaya-Hamada, F., Kanno, H Fujii, H., Yoshida, T., and Miwa, S., A novel human catalase mutation (358 T- del) causing Japanese-type acatalasemia. Blood Cells Mol. Dis. 21, 232-234 (1995). 

The chemistry of the colorful, perplexing, and challenging problem of catalase mechanism has been set forth in numerous reviews. Those by Brill 16), Nicholls and Schonbaum (f ), and most recently, Deisseroth and Bounce (15) summarize the fundamental properties of catalase and its reactions, and their physiological implications. Further, Feinstein 19) and Aebi 20-22) have presented detailed evaluations of acatalasemia, and de Duve 23) and others have discussed catalase biosynthesis 23-26), its intracellular location 23-25) and its turnover 24, 26-28). These facets of the catalase problem will not be reiterated. Instead, a brief synopsis of the enzyme characteristics will be followed by a discussion on the nature of the active site and the chemistry of the catalase reaction mechanism. 

Despite the size of the protein subunits, their integrity does not depend on cross-linking via disulfide bonds (63) and no disulfide bridges have been identified within the partially completed amino acid sequence (41, 6Sa). Nor is there any evidence that association of subunits depends on covalent bonding rather, it appears to involve mainly hydrophobic interactions (50). Of particular interest in this context is the observation that some forms of acatalasemia are attributable to the formation of a catalase variant, of approximately normal specific activity, but with a tendency to dissociate into subunits (64). 

Pseudo-ZeUwegePs syndrome Genetic diseases with a single enzyme defect and a normal number of peroxisomes X"linked adrenoleukodystrophy Adult Refsum s disease Acatalasemia... 

Several rare mutations/polymorphisms have been reported in the CAT gene in humans, most of them being associated with acatalasemia, characterized by erythrocyte CAT levels of 0.2-4% of normal (see Sect. 2.8). A common C-T... 

Treatment of acatalasemia and removal of hydrogen peroxide in human cells Treatment of jaundice Skin ulcers... 

Goth, L., A new type of inherited catalase deficiencies Its characterization and comparison to the Japanese and Swiss type of acatalasemia. Blood Cells Mol. Dis., 27, 512, 2001. 

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