Biology:GSTT2

Generic protein structure example

Glutathione S-transferase theta-2 is an enzyme that in humans is encoded by the GSTT2 gene.

Glutathione S-transferase (GSTs) theta 2 (GSTT2) is a member of a superfamily of proteins that catalyze the conjugation of reduced glutathione to a variety of electrophilic and hydrophobic compounds. Human GSTs can be divided into five main classes: Alpha, Mu, Pi, Theta, and Zeta. The theta class members GSTT1 and GSTT2 share 55% amino acid sequence identity and both are thought to have an important role in human carcinogenesis. The theta genes have a similar structure, being composed of five exons with identical exon/intron boundaries.

Further reading

• "Characterization of a human class-Theta glutathione S-transferase with activity towards 1-menaphthyl sulphate.". Biochem. J. 286 (3): 929–35. 1992. doi:10.1042/bj2860929. PMID 1417752. 
• "Characterization of a cDNA and gene encoding the mouse theta class glutathione transferase mGSTT2 and its localization to chromosome 10B5-C1.". Genomics 33 (1): 105–11. 1996. doi:10.1006/geno.1996.0165. PMID 8617493. 
• "Chromosomal localization of the gene for the human theta class glutathione transferase (GSTT1).". Genomics 33 (1): 121–3. 1996. doi:10.1006/geno.1996.0167. PMID 8617495. 
• "The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human.". Biochem. J. 318 (1): 297–303. 1996. doi:10.1042/bj3180297. PMID 8761485. 
• "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. 1997. doi:10.1101/gr.6.9.791. PMID 8889548. 
• "Homology model for the human GSTT2 Theta class glutathione transferase.". Proteins 27 (1): 118–30. 1997. doi:10.1002/(SICI)1097-0134(199701)27:1<118::AID-PROT12>3.0.CO;2-Q. PMID 9037717. 
• "Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site.". Structure 6 (3): 309–22. 1998. doi:10.1016/S0969-2126(98)00034-3. PMID 9551553. 
• "Expression of glutathione S-transferase theta class isoenzymes in human colorectal and gastric cancers.". Carcinogenesis 20 (8): 1453–7. 1999. doi:10.1093/carcin/20.8.1453. PMID 10426791. 
• "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. 1999. doi:10.1038/990031. PMID 10591208. Bibcode: 1999Natur.402..489D. 
• "Expression of glutathione S-transferase alpha, P1-1 and T1-1 in the human gastrointestinal tract.". Jpn. J. Cancer Res. 91 (3): 310–6. 2000. doi:10.1111/j.1349-7006.2000.tb00946.x. PMID 10760690. 
• "Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation.". Pharmacogenetics 10 (6): 557–65. 2001. doi:10.1097/00008571-200008000-00009. PMID 10975610. 
• "The sequence of the human genome.". Science 291 (5507): 1304–51. 2001. doi:10.1126/science.1058040. PMID 11181995. Bibcode: 2001Sci...291.1304V. 
• "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M. 
• "The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily: suggestion for an evolutionary pressure in the direction of the storage of nitric oxide.". J. Biol. Chem. 278 (43): 42283–93. 2004. doi:10.1074/jbc.M305568200. PMID 12871945. 
• "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. 2005. doi:10.1186/gb-2004-5-10-r84. PMID 15461802. 
• "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334. 
• "GSTT2 promoter polymorphisms and colorectal cancer risk.". BMC Cancer 7: 16. 2007. doi:10.1186/1471-2407-7-16. PMID 17250773.