Difference between revisions of "Glutathione S-transferase omega-1"

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===Protein Function ===
 
===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/>
 
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)
 
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)
 
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Revision as of 05:33, 21 January 2020

Basic Information
Short Name GSTO1
UNP ID P78417
Organism Homo sapiens
Cys Site Cys32
Family/Domain Glutathione S-transferase,
GST superfamily,
Omega family
Known Ligand Ligand list
Function Type 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 is the active site of GSTO1, and very close to the Glutathione binding site Lys59 and Val72 in space.

  • Hydrophobic property:
598-hydro.png
  • SASA:
Cys32: Unknown A^2

Protein Sequence

MSGESARSLG KGSAPPGPVP EGSIRIYSMR FCPFAERTRL 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:
598.png

Related Pathway


Experimental Evidence

Crystallography, MALDI-TOF-MS/MS, Protein Digest assay

Reference

  1. 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. 10783391
  2. Sampayo-Reyes A, Zakharyan R A. Tocopherol esters inhibit human glutathione S-transferase omega[J]. Acta Biochimica Polonica, 2006, 53(3): 547-552. 17019444
  3. 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. 20205472
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