Peroxiredoxin-2 - Revision history

Wu3857: /* Reference */

2019-08-19T23:09:36Z

‎Reference

Wu3857 at 01:38, 4 August 2019

2019-08-04T01:38:46Z

Wu3857 at 20:41, 29 July 2019

2019-07-29T20:41:17Z

Wu3857: /* Reference */

2019-07-28T20:24:59Z

‎Reference

Wu3857: /* Structural Information */

2019-07-28T18:19:05Z

‎Structural Information

Wu3857 at 18:02, 28 July 2019

2019-07-28T18:02:55Z

Wu3857: /* Summary */

2019-07-28T18:02:16Z

‎Summary

Wu3857 at 18:00, 28 July 2019

2019-07-28T18:00:18Z

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|PRDX2|[https://www.uniprot.org/uniprot/P32119 P32119]|Homo sapiens|Cys51, Cys172|[http://pfam.xfam.org/family/P..."

2019-07-28T17:59:36Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|PRDX2|[https://www.uniprot.org/uniprot/P32119 P32119]|Homo sapiens|Cys51, Cys172|[http://pfam.xfam.org/family/P..."

New page

{| align="left"
| __TOC__
|}
{{#invoke:InfoboxforTarget|run|PRDX2|[https://www.uniprot.org/uniprot/P32119 P32119]|Homo sapiens|Cys51, Cys172|[http://pfam.xfam.org/family/PF00578 AhpC/TSA family], Peroxiredoxin family, AhpC/Prx1 subfamily|[[:Category:Peroxiredoxin-2|Ligand list]]}}
==Summary==

===Protein Function ===
Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. (From Uniprot) 

===Cys Function & Property===
Cys51 is the active site of Peroxiredoxin-2. This redox-active residue is conserved in AhpC/TSA family. It considered as a peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin. 
[[File:487-HMMlogo.png|center|800px]]
<div align="center">HMM logo of AphC/TSA family (N-terminal)</div> 

* Hydrophobic property:
:[[File:487-hydro.png||600px]]
* SASA：
:Cys51: Unknown
:Cys172: 32.083

==Protein Sequence==

MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV 
'''C'''PTEIIAFSN RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN 
IPLLADVTRR LSEDYGVLKT DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR 
SVDEALRLVQ AFQYTDEHGE V'''C'''PAGWKPGS DTIKPNVDDS KEYFSKHN 


==Structural Information==
*Known structures with covalent ligands: 
:Unknown 

*Protein structure
[[File:487.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko00480 Glutathione metabolism] 

==Experimental Evidence==
:Homologous Analysis of Sequence, Enzymatic Assay

==Reference==
# Nguyen J B, Pool C D, Wong C Y B, et al. '''Peroxiredoxin-1 from the human hookworm Ancylostoma ceylanicum forms a stable oxidized decamer and is covalently inhibited by conoidin A[J].''' Chemistry & Biology, 2013, 20(8): 991-1001. [https://www.ncbi.nlm.nih.gov/pubmed/?term=23891152 23891152] 

[[Category:Targets|Targets]]
[[Category:Peroxiredoxin family|Peroxiredoxin family]]
[[Category:AhpC/Prx1 subfamily|AhpC/Prx1 subfamily]]
[[Category:Glutathione metabolism|Glutathione metabolism]]

@@ Line 44: / Line 44: @@
 [[Category:Targets]]
-[[Category:Targets|Targets]]
+[[Category:Homo sapiens]]
-[[Category:Homo sapiens|Homo sapiens]]
+[[Category:Redox protein]]
-[[Category:Redox protein|Redox protein]]
+[[Category:Peroxiredoxin family]]
-[[Category:Peroxiredoxin family|Peroxiredoxin family]]
+[[Category:AhpC/Prx1 subfamily]]
-[[Category:AhpC/Prx1 subfamily|AhpC/Prx1 subfamily]]
+[[Category:Glutathione metabolism]]

@@ Line 31: / Line 31: @@
 :Unknown<br/>
-*Protein structure
+*Protein structure:
 [[File:487.png|center|800px]]

@@ Line 9: / Line 9: @@
 ===Cys Function & Property===
-Cys51 is the active site of Peroxiredoxin-2. This redox-active residue is conserved in AhpC/TSA family. It considered as a peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.<br/>
+Cys51 is the active site of Peroxiredoxin-2. This redox-active residue is conserved in AhpC/TSA family. It considered as a peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.<br/><br/>
 [[File:487-HMMlogo.png|center|1000px]]
-<div align="center">HMM logo of AphC/TSA family (N-terminal)</div><br/>
+<div align="center">HMM logo of the AphC/TSA family (N-terminal)</div><br/>
 * Hydrophobic property:

@@ Line 10: / Line 10: @@
 ===Cys Function & Property===
 Cys51 is the active site of Peroxiredoxin-2. This redox-active residue is conserved in AhpC/TSA family. It considered as a peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.<br/>
-[[File:487-HMMlogo.png|center|800px]]
+[[File:487-HMMlogo.png|center|1000px]]
 <div align="center">HMM logo of AphC/TSA family (N-terminal)</div><br/>
@@ Line 18: / Line 18: @@
 :Cys51: Unknown
 :Cys172: 32.083 A^2
 ==Protein Sequence==

@@ Line 2: / Line 2: @@
    | __TOC__
    |}
-{{#invoke:InfoboxforTarget|run|PRDX2|[https://www.uniprot.org/uniprot/P32119 P32119]|Homo sapiens|Cys51, Cys172|[http://pfam.xfam.org/family/PF00578 AhpC/TSA family], Peroxiredoxin family,<br/>AhpC/Prx1 subfamily|[[:Category:Peroxiredoxin-2|Ligand list]]|Antioxidant enzyme}}
+{{#invoke:InfoboxforTarget|run|PRDX2|[https://www.uniprot.org/uniprot/P32119 P32119]|Homo sapiens|Cys51, Cys172|[http://pfam.xfam.org/family/PF00578 AhpC/TSA family], Peroxiredoxin family,<br/>AhpC/Prx1 subfamily|[[:Category:Peroxiredoxin-2|Ligand list]]|Redox protein}}
 ==Summary==
@@ Line 47: / Line 47: @@
 [[Category:Targets|Targets]]
 [[Category:Homo sapiens|Homo sapiens]]
-[[Category:Antioxidant enzyme|Antioxidant enzyme]]
+[[Category:Redox protein|Redox protein]]
 [[Category:Peroxiredoxin family|Peroxiredoxin family]]
 [[Category:AhpC/Prx1 subfamily|AhpC/Prx1 subfamily]]
 [[Category:Glutathione metabolism|Glutathione metabolism]]

Peroxiredoxin-2 - Revision history

Wu3857: /* Reference */

Wu3857 at 01:38, 4 August 2019

Wu3857 at 20:41, 29 July 2019

Wu3857: /* Reference */

Wu3857: /* Structural Information */

Wu3857 at 18:02, 28 July 2019

Wu3857: /* Summary */

Wu3857 at 18:00, 28 July 2019

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|PRDX2|[https://www.uniprot.org/uniprot/P32119 P32119]|Homo sapiens|Cys51, Cys172|[http://pfam.xfam.org/family/P..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|PRDX2|[https://www.uniprot.org/uniprot/P32119 P32119]|Homo sapiens|Cys51, Cys172|[http://pfam.xfam.org/family/P..."