2j2m
CRYSTAL STRUCTURE ANALYSIS OF CATALASE FROM EXIGUOBACTERIUM OXIDOTOLERANS
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OverviewOverview
A catalase that exhibits a high level of activity and a rapid reaction, with organic peroxides has been purified from Exiguobacterium, oxidotolerans T-2-2T (EKTA catalase). The amino acid sequence of EKTA, catalase revealed that it is a novel clade 1 catalase. Amino acid residues, in the active site around the protoheme are conserved in the primary, structure of EKTA catalase. Although the general interactions of molecules, larger than hydrogen peroxide with catalases are strongly inhibited, because of the selection role of long and narrow channels in the substrate, reaching the active site, the formation rate of reactive intermediates, (compound I) in the reaction of EKTA catalase with peracetic acid is 77, times higher than that of bovine liver catalase (BLC) and 1200 times, higher than ... [(full description)]
About this StructureAbout this Structure
2J2M is a [Single protein] structure of sequence from [Exiguobacterium oxidotolerans] with HEM as [ligand]. Active as [Catalase], with EC number [1.11.1.6]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Relationship between the size of the bottleneck 15 A from iron in the main channel and the reactivity of catalase corresponding to the molecular size of substrates., Hara I, Ichise N, Kojima K, Kondo H, Ohgiya S, Matsuyama H, Yumoto I, Biochemistry. 2007 Jan 9;46(1):11-22. PMID:17198371
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