1oag
From Proteopedia
(New page: 200px<br /> <applet load="1oag" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oag, resolution 1.75Å" /> '''ASCORBATE PEROXIDAS...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1OAG is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Glycine_max Glycine max]] with SO4 and HEM as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OAG OCA]]. | + | 1OAG is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Glycine_max Glycine max]] with SO4 and HEM as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/L-ascorbate_peroxidase L-ascorbate peroxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OAG OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of the ascorbate peroxidase-ascorbate complex., Sharp KH, Mewies M, Moody PC, Raven EL, Nat Struct Biol. 2003 Apr;10(4):303-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12640445 12640445] | Crystal structure of the ascorbate peroxidase-ascorbate complex., Sharp KH, Mewies M, Moody PC, Raven EL, Nat Struct Biol. 2003 Apr;10(4):303-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12640445 12640445] | ||
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
| + | [[Category: L-ascorbate peroxidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Moody, P.C.E.]] | [[Category: Moody, P.C.E.]] | ||
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[[Category: peroxide scavenge]] | [[Category: peroxide scavenge]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:54:33 2007'' |
Revision as of 10:49, 30 October 2007
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ASCORBATE PEROXIDASE FROM SOYBEAN CYTOSOL
Overview
Heme peroxidases catalyze the H2O2-dependent oxidation of a variety of, substrates, most of which are organic. Mechanistically, these enzymes are, well characterized: they share a common catalytic cycle that involves, formation of a two-electron, oxidized Compound I intermediate followed by, two single-electron reduction steps by substrate. The substrate, specificity is more diverse--most peroxidases oxidize small organic, substrates, but there are prominent exceptions--and there is a notable, absence of structural information for a representative, peroxidase-substrate complex. Thus, the features that control substrate, specificity remain undefined. We present the structure of the complex of, ascorbate peroxidase-ascorbate. The structure defines the, ascorbate-binding interaction for the ... [(full description)]
About this Structure
1OAG is a [Single protein] structure of sequence from [Glycine max] with SO4 and HEM as [ligands]. Active as [L-ascorbate peroxidase], with EC number [1.11.1.11]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the ascorbate peroxidase-ascorbate complex., Sharp KH, Mewies M, Moody PC, Raven EL, Nat Struct Biol. 2003 Apr;10(4):303-7. PMID:12640445
Page seeded by OCA on Tue Oct 30 12:54:33 2007
