Gamma-Glutamyltransferase Light Chain 2 (gGTLC2)

Gamma-glutamyltransferase-1 (GGT1) is a membrane-bound extracellular enzyme that cleaves gamma-glutamyl peptide bonds in glutathione and other peptides and transfers the gamma-glutamyl moiety to acceptors. Autocatalytic cleavage of the GGT1 precursor polypeptide produces a heavy chain and a light chain that associate with each other to form the functional enzyme. Light chain-only GGTs, such as GGTLC2, contain a region corresponding to the GGT1 light chain, but they lack the membrane-anchoring heavy chain region .

Compared with other GGTs, GGTLC2 has a mutation at the splice donor of an 81-bp intron, resulting in an unspliced intron. RT-PCR detected GGTLC2 expression in sigmoid colon and placenta, with weaker expression in lung and thyroid, but not in other tissues examined.