1oag

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[[Image:1oag.gif|left|200px]]
[[Image:1oag.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1oag |SIZE=350|CAPTION= <scene name='initialview01'>1oag</scene>, resolution 1.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1oag", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1oag| PDB=1oag | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oag OCA], [http://www.ebi.ac.uk/pdbsum/1oag PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oag RCSB]</span>
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}}
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'''ASCORBATE PEROXIDASE FROM SOYBEAN CYTOSOL'''
'''ASCORBATE PEROXIDASE FROM SOYBEAN CYTOSOL'''
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[[Category: Raven, E L.]]
[[Category: Raven, E L.]]
[[Category: Sharp, K H.]]
[[Category: Sharp, K H.]]
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[[Category: ascorbate peroxidase]]
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[[Category: Ascorbate peroxidase]]
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[[Category: heme peroxidase]]
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[[Category: Heme peroxidase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: peroxide scavenge]]
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[[Category: Peroxide scavenge]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:35:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:22 2008''
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Revision as of 00:35, 3 May 2008

Image:1oag.gif

Template:STRUCTURE 1oag

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.

About this Structure

1OAG is a Single protein structure of sequence from Glycine max. 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 Sat May 3 03:35:37 2008

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OCA

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