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1oag
From Proteopedia
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| - | [[Image:1oag.gif|left|200px]]<br /> | + | [[Image:1oag.gif|left|200px]]<br /><applet load="1oag" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1oag" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1oag, resolution 1.75Å" /> | caption="1oag, resolution 1.75Å" /> | ||
'''ASCORBATE PEROXIDASE FROM SOYBEAN CYTOSOL'''<br /> | '''ASCORBATE PEROXIDASE FROM SOYBEAN CYTOSOL'''<br /> | ||
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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/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] | + | 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] Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OAG OCA]. |
==Reference== | ==Reference== | ||
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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 Dec 18 17:15:13 2007'' |
Revision as of 15:05, 18 December 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 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 with SO4 and HEM 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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