User:Tania Girao Mangolini/Sandbox 1
From Proteopedia
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There are sites for N glycosylation in the loop regions, at <scene name='84/845930/Asnnglicosylation/2'>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"/>. | There are sites for N glycosylation in the loop regions, at <scene name='84/845930/Asnnglicosylation/2'>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"/>. | ||
| - | 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> ([ | + | 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> ([http://www.rcsb.org/structure/1HCH 1HCH]), that is the active form of this enzyme. |
| Line 19: | Line 19: | ||
TODO: include image with reactions | TODO: include image with reactions | ||
| - | <scene name='84/845930/Compoundi_oxy/1'>Compound I Oxygen</scene> | + | <scene name='84/845930/Compoundi_oxy/1'>Compound I Oxygen</scene> |
| - | <scene name='84/845930/Compoundii_v2/1'>Compound II</scene> | + | <scene name='84/845930/Compoundii_v2/1'>Compound II</scene> ([http://www.rcsb.org/structure/1H55 1H55]) |
| - | <scene name='84/845930/Compoundiii/1'>Compound III</scene> | + | <scene name='84/845930/Compoundiii/1'>Compound III</scene> ([http://www.rcsb.org/structure/1H57 1H57]) |
<scene name='84/845930/Compoundiii_peroxidases/1'>Compound III Peroxidases</scene> | <scene name='84/845930/Compoundiii_peroxidases/1'>Compound III Peroxidases</scene> | ||
Revision as of 01:12, 1 June 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 the residue at is Ile according to the GenBank entry M37156.1 but Tyr according to the GenBank entry HE963800.1 [2].
The molecule 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, each one with a .
In the center of HRP C1A there is a , which is linked to the molecule by a coordinate bond of the heme iron with a conserved residue [1].
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].
Other residues play essencial roles in the the molecule, as the and , which are related to the formation and stabilization of (1HCH), that is the active form of this enzyme.
The following image shows the HRP C1A's catalytic cycle:
TODO: include image with reactions
(1H55)
(1H57)
References
- ↑ 1.0 1.1 1.2 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 2.2 Krainer, F.W; GLIEDER, A. An updated view on horseradish peroxidases: recombinant production and biotechnological applications v. 99, pages 1611–1625 (2015). DOI: 10.1007/s00253-014-6346-7
