User:Tania Girao Mangolini/Sandbox 1
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | HRP C1A is composed by 308 residues and the amino acid at position 37 is Ile according to the GenBank entry [https://www.ncbi.nlm.nih.gov/nuccore/M37156.1 M37156.1] but Tyr according to the GenBank entry https://www.ncbi.nlm.nih.gov/nuccore/HE963800.1 HE963800.1] <ref name="ref2"/>. | + | HRP C1A is composed by 308 residues and the amino acid at position 37 is Ile according to the GenBank entry [https://www.ncbi.nlm.nih.gov/nuccore/M37156.1 M37156.1] but Tyr according to the GenBank entry [https://www.ncbi.nlm.nih.gov/nuccore/HE963800.1 HE963800.1] <ref name="ref2"/>. |
| - | The molecule 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, each one with a <scene name='84/845930/Calcio/2'>calcium atom</scene>. In the center of HRP C1A 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</scene> residue <ref name="review"/>. | + | The molecule 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, each one with a <scene name='84/845930/Calcio/2'>calcium atom</scene>. |
| + | |||
| + | In the center of HRP C1A 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</scene> residue <ref name="review"/>. | ||
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"/>. | ||
Revision as of 20:22, 15 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 the amino acid at position 37 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 , that is the active form of this enzyme.
The following image shows the HRP C1A's catalytic cycle:
TODO: include image with reactions
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
