User:Tania Girao Mangolini/Sandbox 1

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== Structural highlights ==
== Structural highlights ==
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HRP C1A 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. The molecule is separated into a distal and a proximal region, each one with a <scene name='84/845930/Calcio/1'>calcium atom</scene>. In the center of the molecule there is a <scene name='84/845930/Heme/1'>heme group</scene>, 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="review"\>
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HRP C1A 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. The molecule is separated into a distal and a proximal region, each one with a <scene name='84/845930/Calcio/1'>calcium atom</scene>. In the center of the molecule there is a <scene name='84/845930/Heme/1'>heme group</scene>, 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="review"/>

Revision as of 22:12, 14 May 2020

HORSERADISH PEROXIDASE C1A

PDB entry 1H58

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Horseadish (Armoracia rusticana) is a plant that belongs 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 C1A is composed by 308 residues and has a predominantly α-helical , with the exception of one short β-sheet region. The molecule is separated into a distal and a proximal region, each one with a . In the center of the molecule there is a , which is linked to the molecule by a coordinate bond of the heme iron with a conserved [1]


TODO: include image with reactions

References

  1. ↑ 1.0 1.1 Veitch, N.C. Horseadich peroxidase: a modern view of a classic enzyme 65:249-259 (2004). DOI: 10.1016/j.phytochem.2003.10.022
  2. ↑ 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

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Tania Girao Mangolini

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