1oaf
From Proteopedia
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| - | [[Image:1oaf.gif|left|200px]]<br /><applet load="1oaf" size=" | + | [[Image:1oaf.gif|left|200px]]<br /><applet load="1oaf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oaf, resolution 1.4Å" /> | caption="1oaf, resolution 1.4Å" /> | ||
'''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE'''<br /> | '''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OAF 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 NA, HEM and ASC 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] Known structural/functional Site: <scene name='pdbsite=AC1:Asc Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1OAF 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 <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=ASC:'>ASC</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Asc+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peroxide scavenge]] | [[Category: peroxide scavenge]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:55:33 2008'' |
Revision as of 07:55, 3 February 2008
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ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE
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
1OAF is a Single protein structure of sequence from Glycine max with , and as ligands. Active as L-ascorbate peroxidase, with EC number 1.11.1.11 Known structural/functional Site: . 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
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