User:Tania Girao Mangolini/Sandbox 1
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | 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/2'>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> | + | 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/2'>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>. |
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Other residues play essencial roles in the the molecule, as the <scene name='84/845930/Arg38/2'>Arg38</scene> and <scene name='84/845930/Hist42/1'>His42</scene>, which are related to the formation and stabilization of <scene name='84/845930/Compoundi/1'>Compound I</scene>, that is the active form of this enzyme. | Other residues play essencial roles in the the molecule, as the <scene name='84/845930/Arg38/2'>Arg38</scene> and <scene name='84/845930/Hist42/1'>His42</scene>, which are related to the formation and stabilization of <scene name='84/845930/Compoundi/1'>Compound I</scene>, that is the active form of this enzyme. | ||
| - | There are sites for N glycosylation in the loop regions, at Asn13, Asn57, Asn58, Asn186, Asn198, Asn214, Asn255 and Asn268 | + | |
| + | There are sites for N glycosylation in the loop regions, at <scene name='84/845930/Asnnglicosylation/1'>Asn13, Asn57, Asn58, Asn186, Asn198, Asn214, Asn255 and Asn268</scene> residues<ref name="review"/>. All these glycosylated Asn residues are located on the surface of C1A<ref name="ref2"/>. | ||
The following image shows the HRP C1A's catalytic cycle: | The following image shows the HRP C1A's catalytic cycle: | ||
Revision as of 22:57, 14 May 2020
HORSERADISH PEROXIDASE C1A
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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 .
Other residues play essencial roles in the the molecule, as the and , which are related to the formation and stabilization of , that is the active form of this enzyme.
There are sites for N glycosylation in the loop regions, at residues[1]. All these glycosylated Asn residues are located on the surface of C1A[2].
The following image shows the HRP C1A's catalytic cycle: TODO: include image with reactions
References
- ↑ 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
- ↑ 2.0 2.1 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
