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Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis

1999; Elsevier BV; Volume: 72; Issue: 1 Linguagem: Inglês

10.1016/s0079-6107(98)00058-3

1873-1732

Marcel Zámocký, Franz Koller,

Protein Interaction Studies and Fluorescence Analysis

This review gives an overview about the structural organisation of different evolutionary lines of all enzymes capable of efficient dismutation of hydrogen peroxide. Major potential applications in biotechnology and clinical medicine justify further investigations. According to structural and functional similarities catalases can be divided in three subgroups. Typical catalases are homotetrameric haem proteins. The three-dimensional structure of six representatives has been resolved to atomic resolution. The central core of each subunit reveals a chracteristic ``catalase fold'', extremely well conserved among this group. In the native tetramer structure pairs of subunits tightly interact via exchange of their N-terminal arms. This pseudo-knot structures implies a highly ordered assembly pathway. A minor subgroup (``large catalases'') possesses an extra flavodoxin-like C-terminal domain. A ≥25Å long channel leads from the enzyme surface to the deeply buried active site. It enables rapid and selective diffusion of the substrates to the active center. In several catalases NADPH is tightly bound close to the surface. This cofactor may prevent and reverse the formation of compound II, an inactive reaction intermediate. Bifunctional catalase-peroxidases are haem proteins which probably arose via gene duplication of an ancestral peroxidase gene. No detailed structural information is currently available. Even less is know about manganese catalases. Their di-manganese reaction centers may be evolutionary related to manganese centers in photosystem II. Current research in this field focuses mainly on stress-regulation of catalase expression, on the role of catalases in plant defense, and on in vivo and in vitro folding of catalases.