This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1oaf
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1oaf.gif|left|200px]] | [[Image:1oaf.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1oaf", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1oaf| PDB=1oaf | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE''' | '''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH ASCORBATE''' | ||
| Line 29: | Line 26: | ||
[[Category: Raven, E L.]] | [[Category: Raven, E L.]] | ||
[[Category: Sharp, K H.]] | [[Category: Sharp, K H.]] | ||
| - | [[Category: | + | [[Category: Ascorbate peroxidase]] |
| - | [[Category: | + | [[Category: Heme peroxidase]] |
| - | [[Category: | + | [[Category: Peroxide scavenge]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:35:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:35, 3 May 2008
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. 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 03:35:41 2008
