1oag
ASCORBATE PEROXIDASE FROM SOYBEAN CYTOSOL
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OverviewOverview
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 ... [(full description)]
About this StructureAbout 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]. Structure known Active Site: AC1. 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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