User:Tania Girao Mangolini/Sandbox 1
From Proteopedia
(Difference between revisions)
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<Structure load='1h58' size='350' frame='true' align='right' caption='PDB entry [[1H58]]' scene='84/845930/Hrp_c1a/2' /> | <Structure load='1h58' size='350' frame='true' align='right' caption='PDB entry [[1H58]]' scene='84/845930/Hrp_c1a/2' /> | ||
Horseadish ([http://en.wikipedia.org/wiki/Horseradish ''Armoracia rusticana'']) is a plant belonging to the [http://en.wikipedia.org/wiki/Brassicaceae Brassicaceae] family. The roots of this plant are rich in [http://en.wikipedia.org/wiki/Peroxidase peroxidases], being the HRP C [http://en.wikipedia.org/wiki/Isozyme isozymes] the most common ones. <ref name="review">Veitch, N.C. Horseadich peroxidase: a modern view of a classic enzyme 65:249-259 (2004). [https://doi.org/10.1016/j.phytochem.2003.10.022 DOI: 10.1016/j.phytochem.2003.10.022]</ref> | Horseadish ([http://en.wikipedia.org/wiki/Horseradish ''Armoracia rusticana'']) is a plant belonging to the [http://en.wikipedia.org/wiki/Brassicaceae Brassicaceae] family. The roots of this plant are rich in [http://en.wikipedia.org/wiki/Peroxidase peroxidases], being the HRP C [http://en.wikipedia.org/wiki/Isozyme isozymes] the most common ones. <ref name="review">Veitch, N.C. Horseadich peroxidase: a modern view of a classic enzyme 65:249-259 (2004). [https://doi.org/10.1016/j.phytochem.2003.10.022 DOI: 10.1016/j.phytochem.2003.10.022]</ref> | ||
| - | However, most of the HRP research has focused on one isozyme: HRP C1A | + | However, most of the HRP research has focused on one isozyme: <scene name='84/845930/Hrp_c1a/2'>HRP C1A</scene> <ref name="ref2">Krainer, F.W; GLIEDER, A. An updated view on horseradish peroxidases: recombinant production and biotechnological applications 99, pages1611–1625(2015). [https://doi.org/10.1007/s00253-014-6346-7 DOI: 10.1007/s00253-014-6346-7]</ref> |
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| - | TODO: include image with reactions | ||
== Structural highlights == | == Structural highlights == | ||
| - | 308 residues | + | HRP is composed by 308 residues and has a predominantly α-helical <scene name='84/845930/1h58_secondary_structure/1'>secondary structure</scene> with the exception of one short β-sheet region and it is separated into a distal and a proximal region by a <scene name='84/845930/Heme/1'>heme</scene> group, which is linked to the molecule by a coordinate bond of the heme iron with a conserved <scene name='84/845930/His170_v2/2'>His170 residue </scene><ref name="ref2"></ref> |
| - | + | TODO: include image with reactions | |
| - | <scene name='84/845930/1h58_secondary_structure/1'>1H58_secondary_structure</scene> | ||
| - | <scene name='84/845930/ | + | <scene name='84/845930/Calcio/1'>Calcio</scene> |
| - | <scene name='84/845930/Calcio/1'>Calcio</scene> | ||
| - | <scene name='84/845930/His170_v2/2'>His170</scene> | ||
<scene name='84/845930/Arg38/2'>Arg38</scene> | <scene name='84/845930/Arg38/2'>Arg38</scene> | ||
Revision as of 21:54, 14 May 2020
HORSERADISH PEROXIDASE C1A
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Horseadish (Armoracia rusticana) is a plant belonging to the Brassicaceae family. The roots of this plant are rich in peroxidases, being the HRP C isozymes the most common ones. [1] However, most of the HRP research has focused on one isozyme: [2]
Structural highlights
HRP is composed by 308 residues and has a predominantly α-helical with the exception of one short β-sheet region and it is separated into a distal and a proximal region by a group, which is linked to the molecule by a coordinate bond of the heme iron with a conserved Cite error: Invalid <ref> tag;
refs with no name must have content
TODO: include image with reactions
References
- ↑ Veitch, N.C. Horseadich peroxidase: a modern view of a classic enzyme 65:249-259 (2004). DOI: 10.1016/j.phytochem.2003.10.022
- ↑ Krainer, F.W; GLIEDER, A. An updated view on horseradish peroxidases: recombinant production and biotechnological applications 99, pages1611–1625(2015). DOI: 10.1007/s00253-014-6346-7
