Ascorbate peroxidase
From Proteopedia
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- | + | <StructureSection load='1oaf' size='350' side='right' scene='48/486478/Cv/1' caption='Soybean heme-containing ascorbate peroxidase complex with ascorbate and Na+ ion (purple), [[1oaf]]'> | |
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== Function == | == Function == | ||
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APX is part of plants antioxidant defense. APX converts H2O2 to water using ascorbate as an electron donor. APX is used in electron microscopy as a genetic tag which can be stained independently of light activation. | APX is part of plants antioxidant defense. APX converts H2O2 to water using ascorbate as an electron donor. APX is used in electron microscopy as a genetic tag which can be stained independently of light activation. | ||
- | == | + | == Structural highlights == |
- | + | The <scene name='48/486478/Cv/4'>heme-containing active site</scene> of APX contains a <scene name='48/486478/Cv/5'>His residue (H163 in soybean) which coordinates with the heme</scene> and confers stability to the Fe state in the heme. <ref>PMID:12640445</ref> | |
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- | + | ==3D structures of ascorbate peroxidase== | |
- | + | [[Ascorbate peroxidase 3D structures]] | |
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- | + | </StructureSection> | |
- | + | == References == | |
- | + | <references/> | |
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[[Category:Topic Page]] | [[Category:Topic Page]] |
Current revision
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References
- ↑ Sharp KH, Mewies M, Moody PC, Raven EL. Crystal structure of the ascorbate peroxidase-ascorbate complex. Nat Struct Biol. 2003 Apr;10(4):303-7. PMID:12640445 doi:http://dx.doi.org/10.1038/nsb913