2j2m
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 2J2M is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Exiguobacterium_oxidotolerans Exiguobacterium oxidotolerans]] with HEM as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | + | 2J2M is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Exiguobacterium_oxidotolerans Exiguobacterium oxidotolerans]] with HEM as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Catalase Catalase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J2M OCA]]. |
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17198371 17198371] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17198371 17198371] | ||
| + | [[Category: Catalase]] | ||
[[Category: Exiguobacterium oxidotolerans]] | [[Category: Exiguobacterium oxidotolerans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:27:19 2007'' |
Revision as of 08:22, 30 October 2007
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CRYSTAL STRUCTURE ANALYSIS OF CATALASE FROM EXIGUOBACTERIUM OXIDOTOLERANS
Overview
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 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].
Reference
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
Page seeded by OCA on Tue Oct 30 10:27:19 2007
