background:
g-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 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.
Function:
Cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. Converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4).
Subunit:
Heterodimer composed of the light and heavy chains. The active site is located in the light chain
Subcellular Location:
Membrane; Single-pass type II membrane protein.
Similarity:
Belongs to the gamma-glutamyltransferase family.
Database links:
UniProtKB/Swiss-Prot: P36269.2
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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