Glutathione S-transferase omega-1 - Revision history

Wu3857: /* Cys Function & Property */

2020-01-21T05:33:29Z

‎Cys Function & Property

Wu3857: /* Protein Function */

2020-01-21T05:33:17Z

‎Protein Function

Wu3857: /* Cys Function & Property */

2020-01-21T05:30:44Z

‎Cys Function & Property

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|GSTO1|[https://www.uniprot.org/uniprot/P78417 P78417]|Homo sapiens|Cys32|[http://pfam.xfam.org/family/PF13417 G..."

2020-01-21T05:29:35Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|GSTO1|[https://www.uniprot.org/uniprot/P78417 P78417]|Homo sapiens|Cys32|[http://pfam.xfam.org/family/PF13417 G..."

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{{#invoke:InfoboxforTarget|run|GSTO1|[https://www.uniprot.org/uniprot/P78417 P78417]|Homo sapiens|Cys32|[http://pfam.xfam.org/family/PF13417 Glutathione S-transferase], GST superfamily, Omega family|[[:Category:Glutathione S-transferase omega-1|Ligand list]]|Metabolic enzyme}}
==Summary==

===Protein Function ===
Glutathione S-transferases (GSTs) are a family of phase II detoxification enzymes that conjugate reduced glutathione (GSH) to various electrophilic compounds. GSTs are abundant in cells (making up to 10% of cytosolic protein) and consist of at least seven subfamilies such as alpha, kappa, mu, pi, theta, zeta, and omega, and each subclass has several isoforms, respectively. The omega GSTs (GSTO1 and GSTO2) are a subfamily harboring a cysteine residue in their active site, whereas the other subfamilies have a serine or tyrosine residue. (PMID: 20205472) 
GSTO1 is suspected to be involved in certain cancers and neurodegenerative diseases. GSTO1 exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. It also has S-(phenacyl)glutathione reductase and also glutathione S-transferase activity. It could participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. (From Uniprot)
 

===Cys Function & Property===
The Cys32 in GSTO1 is the active site, and very close to the Glutathione binding site Lys59 and Val72. 

* Hydrophobic property:
:[[File:598-hydro.png||600px]]
* SASA:
:Cys32: Unknown A^2 

==Protein Sequence==

MSGESARSLG KGSAPPGPVP EGSIRIYSMR F'''C'''PFAERTRL VLKAKGIRHE 
VININLKNKP EWFFKKNPFG LVPVLENSQG QLIYESAITC EYLDEAYPGK 
KLLPDDPYEK ACQKMILELF SKVPSLVGSF IRSQNKEDYA GLKEEFRKEF 
TKLEEVLTNK KTTFFGGNSI SMIDYLIWPW FERLEAMKLN ECVDHTPKLK 
LWMAAMKEDP TVSALLTSEK DWQGFLELYL QNSPEACDYG L 


==Structural Information==
*Known structure with covalent ligand: 
:Unknown 

*Protein structure:
[[File:598.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko00480 Glutathione metabolism] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko00980 Metabolism of xenobiotics by cytochrome P450] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko00982 Drug metabolism - cytochrome P450] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko00983 Drug metabolism - other enzymes] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko01100 Metabolic pathways] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko01524 Platinum drug resistance] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05200 Pathways in cancer] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05204 Chemical carcinogenesis] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05225 Hepatocellular carcinoma] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05418 Fluid shear stress and atherosclerosis] 

==Experimental Evidence==
:Crystallography, MALDI-TOF-MS/MS, Protein Digest assay

==Reference==
# Board P G, Coggan M, Chelvanayagam G, et al. '''Identification, characterization, and crystal structure of the Omega class glutathione transferases[J].''' Journal of Biological Chemistry, 2000, 275(32): 24798-24806. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10783391 10783391] 
# Sampayo-Reyes A, Zakharyan R A. '''Tocopherol esters inhibit human glutathione S-transferase omega[J].''' Acta Biochimica Polonica, 2006, 53(3): 547-552. [https://www.ncbi.nlm.nih.gov/pubmed/?term=17019444 17019444] 
# Son J, Lee J J, Lee J S, et al. '''Isozyme-specific fluorescent inhibitor of glutathione s-transferase omega 1[J].''' ACS chemical biology, 2010, 5(5): 449-453. [https://www.ncbi.nlm.nih.gov/pubmed/?term=20205472 20205472] 

[[Category:Targets]]
[[Category:Homo sapiens]]
[[Category:Metabolic enzyme]]
[[Category:GST superfamily]]
[[Category:Omega family]]
[[Category:Glutathione metabolism]]
[[Category:Metabolism of xenobiotics by cytochrome P450]]
[[Category:Drug metabolism - cytochrome P450]]
[[Category:Drug metabolism - other enzymes]]
[[Category:Metabolic pathways]]
[[Category:Platinum drug resistance]]
[[Category:Pathways in cancer]]
[[Category:Chemical carcinogenesis]]
[[Category:Hepatocellular carcinoma]]
[[Category:Fluid shear stress and atherosclerosis]]

@@ Line 12: / Line 12: @@
 ===Cys Function & Property===
-The Cys32 is the active site of GSTO1, and very close to the Glutathione binding site Lys59 and Val72 in space.<br/>
+The Cys32 is the active site of GSTO1, and very close to the Glutathione binding sites Lys59 and Val72 in space.<br/>
 * Hydrophobic property:

@@ Line 11: / Line 11: @@
 ===Cys Function & Property===
-The Cys32 in GSTO1 is the active site, and very close to the Glutathione binding site Lys59 and Val72.<br/>
+The Cys32 is the active site of GSTO1, and very close to the Glutathione binding site Lys59 and Val72 in space.<br/>
 * Hydrophobic property:

@@ Line 7: / Line 7: @@
 ===Protein Function ===
 Glutathione S-transferases (GSTs) are a family of phase II detoxification enzymes that conjugate reduced glutathione (GSH) to various electrophilic compounds. GSTs are abundant in cells (making up to 10% of cytosolic protein) and consist of at least seven subfamilies such as alpha, kappa, mu, pi, theta, zeta, and omega, and each subclass has several isoforms, respectively. The omega GSTs (GSTO1 and GSTO2) are a subfamily harboring a cysteine residue in their active site, whereas the other subfamilies have a serine or tyrosine residue. (PMID: 20205472)<br/>
 GSTO1 is suspected to be involved in certain cancers and neurodegenerative diseases. GSTO1 exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. It also has S-(phenacyl)glutathione reductase and also glutathione S-transferase activity. It could participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. (From Uniprot)
 <br/>

Glutathione S-transferase omega-1 - Revision history

Wu3857: /* Cys Function & Property */

Wu3857: /* Protein Function */

Wu3857: /* Cys Function & Property */

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|GSTO1|[https://www.uniprot.org/uniprot/P78417 P78417]|Homo sapiens|Cys32|[http://pfam.xfam.org/family/PF13417 G..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|GSTO1|[https://www.uniprot.org/uniprot/P78417 P78417]|Homo sapiens|Cys32|[http://pfam.xfam.org/family/PF13417 G..."