2cag
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 2CAG is a | + | 2CAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 2CAG with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb57_1.html Catalase]]. 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 Sites: DH and PT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CAG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:32:35 2007'' |
Revision as of 13:27, 5 November 2007
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CATALASE COMPOUND II
Overview
Various enzymes use semi-stable ferryl intermediates and free radicals, during their catalytic cycle, amongst them haem catalases. Structures for, two transient intermediates (compounds I and II) of the NADPH-dependent, catalase from Proteus mirabilis (PMC) have been determined by, time-resolved X-ray crystallography and single crystal, microspectrophotometry. The results show the formation and transformation, of the ferryl group in the haem, and the unexpected binding of an anion, during this reaction at a site distant from the haem.
About this Structure
2CAG is a Single protein structure of sequence from Proteus mirabilis with HEM as ligand. The following page contains interesting information on the relation of 2CAG with [Catalase]. Active as Catalase, with EC number 1.11.1.6 Structure known Active Sites: DH and PT. Full crystallographic information is available from OCA.
Reference
Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy., Gouet P, Jouve HM, Williams PA, Andersson I, Andreoletti P, Nussaume L, Hajdu J, Nat Struct Biol. 1996 Nov;3(11):951-6. PMID:8901874
Page seeded by OCA on Mon Nov 5 15:32:35 2007
Categories: Catalase | Proteus mirabilis | Single protein | Gouet, P. | Hajdu, J. | Jouve, H.M. | HEM | Heme | Hydrogen peroxide | Iron | Nadp | Oxidoreductase (h2o2 acceptor) | Peroxidase
