1oag: Difference between revisions

Revision as of 03:59, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1oag.png

Template:STRUCTURE 1oag

ASCORBATE PEROXIDASE FROM SOYBEAN CYTOSOLASCORBATE PEROXIDASE FROM SOYBEAN CYTOSOL

Template:ABSTRACT PUBMED 12640445

About this StructureAbout this Structure

1OAG is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

ReferenceReference

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

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-[[Image:1oag.gif|left|200px]]
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-'''ASCORBATE PEROXIDASE FROM SOYBEAN CYTOSOL'''
+===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 first time and provides new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, which has been a benchmark for peroxidase catalysis for more than 20 years. A new mechanism for electron transfer is proposed that challenges existing views of substrate oxidation in other peroxidases.
+The line below this paragraph, {{ABSTRACT_PUBMED_12640445}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12640445}}
 ==About this Structure==
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 [[Category: Oxidoreductase]]
 [[Category: Peroxide scavenge]]
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