Gamma-glutamyltranspeptidase (GGT) acts as a glutathionase and catalyzes the transfer of the glutamyl moiety of glutathione to a variety of amino acids and dipeptide acceptors. This enzyme is located on the outer surface of the cell membrane and is widely distributed in mammalian tissues involved in absorption and secretion. In humans, hepatic GGT activity is elevated in some liver diseases. GGT1 is released into the bloodstream after liver damage, and an elevated level of the enzyme may be a useful early sign of hepatocellular carcinoma. GGT5 converts leukotriene C4 to leukotriene D4; it does not, however, convert synthetic substrates that are commonly used to assay GGT. In human serum and in human tissues, there is a marked heterogeneity in GGT, but this heterogeneity can be attributed to different glycosylation of the same peptide rather than to the products of different genes. Belonging to the gamma-glutamyltranspeptidase family, GGT6 (gamma-glutamyltransferase 6), is a 493 amino acid single-pass type II membrane protein that cleaves glutathione conjugates. GGT6 exists as two alternatively spliced isoforms.