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Protein-glutamine gamma-glutamyltransferase Z (TGM7) is an enzyme belonging to the transglutaminase family, which catalyzes the calcium-dependent cross-linking of proteins by forming covalent gamma-glutamyl-epsilon-lysine isopeptide bonds and conjugating polyamines to proteins[2][6]. This enzymatic activity stabilizes protein assemblies and modifies protein structure or function, contributing to various physiological processes primarily in testis and lung, but TGM7 expression is considered ubiquitous[1][4]. The precise biological functions of TGM7 are not fully understood, but similar enzymes in the family are involved in cell adhesion, matrix stabilization, and regulation of cellular fate. Disease associations for TGM7 specifically are rare, but mutations and dysregulation of related transglutaminases have roles in genetic and autoimmune conditions[2][1].
Inhibitors of transglutaminase activity (no drugs directly confirmed for TGM7; this is inferred from knowledge of TG enzyme family)
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