Cellular and Molecular Life Sciences CMLS

, Volume 61, Issue 2, pp 192–208 | Cite as

Diversity of structures and properties among catalases

  • P. Chelikani
  • I. Fita
  • P. C. Loewen
Review Paper


More than 300 catalase sequences are now available, divided among monofunctional catalases (> 225), bifunctional catalase-peroxidases (> 50) and manganese-containing catalases (> 25). When combined with the recent appearance of crystal structures from at least two representatives from each of these groups (nine from the monofunctional catalases), valuable insights into the catalatic reaction mechanism in its various forms and into catalase evolution have been gained. The structures have revealed an unusually large number of modifications unique to catalases, a result of interacting with reactive oxygen species. Biochemical and physiological characterization of catalases from many different organisms has revealed a surprisingly wide range of catalatic efficiencies, despite similar sequences. Catalase gene expression in micro-organisms generally is controlled either by sensors of reactive oxygen species or by growth phase regulons, although the detailed mechanisms vary considerably.

Catalase peroxidase crystal structure heme dimanganese 


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Copyright information

© Birkhäuser-Verlag Basel 2004

Authors and Affiliations

  1. 1.Department of MicrobiologyUniversity of ManitobaWinnipeg MBCanada
  2. 2.Institut de BiologÍa Molecular de BarcelonaConsejo Superior de Investigaciones CientÍficasBarcelonaSpain

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