Catalase: A repertoire of unusual features |
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| Authors: | Prashen Chelikani T Ramana T M Radhakrishnan |
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| Institution: | (1) Department of Biology, Massachusetts Institute of Technology, 02139 Cambridge, MA, U.S.A;(2) Biotechnology division, Andhra University, 530 003 Visakhapatnam, AP, India;(3) Rm 68-688D, Dept of Biology, Massachusetts Institute of Technology, 31 Ames Street, 02139 Cambridge, MA, USA |
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| Abstract: | Catalases are antioxidant enzymes which catalyze the breakdown of hydrogen peroxide to water and oxygen, and are one of the
oldest enzymes to be studied biochemically. The first crystal structure of a catalase appeared in the year 1980 and it revealed
the tetrameric nature of the enzyme and presence of channels accessing the deeply buried active site heme. An interesting
feature of the tetrameric structure is the characteristic interweaving or arm exchange of the subunits. The recent elucidation
of the crystal structure of transport proteins (porins, aquaporins) showed that these proteins are also tetrameric in nature
and posses channels. However, recent specific investigations focusing on the roles for these channels, in the mechanism of
enzyme action of catalases, revealed significant similarities with that observed for the transport of water and/or glycerol,
in aquaporins. |
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| Keywords: | Aquaporins Catalases Channels |
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