γ-glutamyl transferase

γ-GT (H-GLA(PNA)-OH) is used as a synthetic substrate for gamma-glutamyltransferase (GGT) to determine GGT activity.

GGTI 2147 FA, a selective GGT inhibitor, abolishes bicuculline-induced increase in dendritic spine density in hippocampal experiments and may reduce learning and memory abilities in mice.

Gamma-Glutamyl Transferase, Human (EC 2.3.2.2) is an enzyme capable of transferring γ-glutamyl functional groups. It catalyzes the transfer of the γ-glutamyl group from glutathione to an acceptor, which can be an amino acid, a peptide, or water (resulting in the production of glutamate).

GPNA hydrochloride is specific glutamine (Gln) transporter ASCT2(SLC1A5) inhibitor. GPNA reversibly induces apoptosis in A549 cells. GPNA hydrochloride is a well-known substrate of the enzyme γ-glutamyltransferase (GGT). GPNA hydrochloride also inhibits

Gamma-Glutamyl Transferase-IN-2 (compound 4dq), a β-carboline 1-hydrazide inhibitor, exhibits antifungal and antibacterial properties by targeting glutamyltransferase, inducing reactive oxygen species accumulation, compromising cell membranes, and disrupting histone acetylation processes [1].

Gamma-Glutamyl Transferase-IN-1 (compound 4de), a β-carboline 1-hydrazide inhibitor, exhibits antifungal and antibacterial properties by targeting glutamyltransferase, inducing reactive oxygen species accumulation, disrupting cell membranes, and dysregulating histone acetylation [1].

γ-glutamyltransferase (GGT) is an enzyme located on the outer surface of the cell membrane. It maintains physiological concentrations of intracellular glutathione and cellular defense against oxidative stress by cleaving extracellular glutathione and increasing the availability of amino acids. γ-glutamyltransferase can be utilized as a biomaterial or organic compound in life science-related research.

OU749 is a γ-glutamyl transferase (GGT) inhibitor with an intrinsic Ki of 17.6 μM.

Protein conjugates in tissue regeneration 2 (PCTR2) is a specialized pro-resolving mediator (SPM) synthesized from docosahexaenoic acid . DHA is oxidized to 16S,17S-epoxy-protectin, which is converted to PCTR1 by glutathione S-transferase and to PCTR2 via γ-glutamyl transpeptidase. PCTR2 is found in resolving mouse exudate and in both M1 and M2 macrophages differentiated from isolated human monocytes.

Maresin conjugates in tissue regeneration 2 (MCTR2) is a specialized pro-resolving mediator (SPM) synthesized from docosahexaenoic acid in macrophages at the site of inflammation. DHA is oxidized to maresin 1 , which is converted to MCTR1 by glutathione S-transferase Mu 4 or leukotriene C4 synthase then to MCTR2 by γ-glutamyl transferase. MCTR2 accelerates tissue regeneration in planaria (1 and 100 nM). Pretreatment with MCTR2 prior to E. coli administration reduces neutrophil infiltration, shortens the inflammatory resolution period, and increases phagocytosis of E. coli by macrophages. When administered at a dose of 100 ng 12h post E. coli infection in a mouse model of peritonitis, MCTR2 selectively reduced the amount of the eicosanoids PGD2 and PGF2α in the exudate.

Maresin conjugates in tissue regeneration 3 (MCTR3) is a specialized pro-resolving mediator (SPM) synthesized from docosahexaenoic acid in macrophages. DHA is oxidized to maresin 1 , which is converted to MCTR1 by glutathione S-transferase Mu 4 or leukotriene C4 synthase, then to MCTR2 by γ-glutamyl transferase, and to MCTR3 by dipeptidase. MCTR3 accelerates tissue regeneration in planaria (1 and 100 nM) approximately as potently as MCTR2 and more potently than MCTR1. Pretreatment with MCTR3 prior to E. coli administration in mice reduces neutrophil infiltration, shortens the inflammatory resolution period, and increases phagocytosis of E. coli by macrophages. When administered at a dose of 100 ng 12h post E. coli infection in a mouse model of peritonitis, MCTR3 selectively reduces the amount of the eicosanoids PGD2 , PGE2 , PGF2α , and TXB2 in the exudate.