GSTT1 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
Aliases | GSTT1 , glutathione S-transferase theta 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 600436 GeneCards: GSTT1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Glutathione S-transferase theta-1 is an enzyme that in humans is encoded by the GSTT1 gene. [2]
Glutathione S-transferase (GST) theta 1 (GSTT1) 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 includes GSTT1 and GSTT2. The GSTT1 and GSTT2 share 55% amino acid sequence identity and both of them were claimed to have an important role in human carcinogenesis. The GSTT1 gene is located approximately 50kb away from the GSTT2 gene. The GSTT1 and GSTT2 genes have a similar structure, being composed of five exons with identical exon/intron boundaries. [3]
A transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups from one molecule to another. They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes.
Glutathione S-transferases (GSTs), previously known as ligandins, are a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies: the cytosolic, mitochondrial, and microsomal—also known as MAPEG—proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new GST functions.
Glutathione S-transferase Mu 1 is a human glutathione S-transferase.
Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene.
Glutathione S-transferase A1 is an enzyme that in humans is encoded by the GSTA1 gene.
In enzymology, maleylacetoacetate isomerase is an enzyme that catalyzes the chemical reaction
Glutathione S-transferase, C-terminal domain is a structural domain of glutathione S-transferase (GST).
Glutathione S-transferase A2 is an enzyme that in humans is encoded by the GSTA2 gene.
Glutathione S-transferase Mu 2 is an enzyme that in humans is encoded by the GSTM2 gene.
Glutathione S-transferase M3 (brain), also known as GSTM2, is an enzyme which in humans is encoded by the GSTM99
Glutathione S-transferase A4, also known as GSTA4, is an enzyme which in humans is encoded by the GSTA4 gene.
Glutathione S-transferase theta-2 is an enzyme that in humans is encoded by the GSTT2 gene.
Glutathione S-transferase Zeta 1 is an enzyme that in humans is encoded by the GSTZ1 gene on chromosome 14.
Glutathione S-transferase Mu 4 is an enzyme that in humans is encoded by the GSTM4 gene.
Microsomal glutathione S-transferase 1 is an enzyme that in humans is encoded by the MGST1 gene.
Glutathione S-transferase omega-1 is an enzyme that in humans is encoded by the GSTO1 gene.
Glutathione S-transferase kappa 1 (GSTK1) is an enzyme that in humans is encoded by the GSTK1 gene which is located on chromosome seven. It belongs to the superfamily of enzymes known as glutathione S-transferase (GST), which are mainly known for cellular detoxification. The GSTK1 gene consists of eight exons and seven introns and although it is a member of the GST family, its structure has been found to be similar to bacterial HCCA (2-hydroxychromene-2-carboxylate) isomerases and bacterial disulphide-bond-forming DsbA oxidoreductase. This similarity has later allowed the enzyme GSTK1 to be renamed to DsbA-L. Research has also suggested that several variations of the GSTK1 gene can be responsible for metabolic diseases and certain types of cancer.
Glutathione S-transferase A3 is an enzyme that in humans is encoded by the GSTA3 gene.
Microsomal glutathione S-transferase 2 is an enzyme that in humans is encoded by the MGST2 gene.
Bacterial glutathione transferases are part of a superfamily of enzymes that play a crucial role in cellular detoxification. The primary role of GSTs is to catalyze the conjugation of glutathione (GSH) with the electrophilic centers of a wide variety of molecules. The most commonly known substrates of GSTs are xenobiotic synthetic chemicals. There are also classes of GSTs that utilize glutathione as a cofactor rather than a substrate. Often these GSTs are involved in reduction of reactive oxidative species toxic to the bacterium. Conjugation with glutathione receptors reders toxic substances more soluble, and therefore more readily exocytosed from the cell.