GLYAT Human

GLYAT belongs to the Gcn5-related N-acetyltransferase (GNAT) superfamily . Despite the low sequence identity among members of this family, the catalytic domain’s topology is conserved. The enzyme’s structure includes additional structural elements that significantly alter the substrate binding site’s architecture and the mechanisms for deprotonation of the primary amine to promote nucleophilic attack .

The enzyme’s primary function is to participate in phase II detoxification by conjugating benzoyl-CoA to glycine to form hippurate, one of the most abundant metabolites in urine . This process is essential for the homeostasis of hepatic and renal CoA, which would otherwise be sequestered as benzoyl-CoA .

GLYAT has been linked to several pathologies in humans, including cancer . Polymorphisms in the GLYAT gene have been associated with variations in musculoskeletal growth, and its expression is downregulated in liver and breast cancer cells . The enzyme’s role in detoxification and metabolism makes it a potential biomarker for various diseases and conditions.

To study GLYAT’s structure and function, the enzyme has been recombinantly expressed and purified from various sources, including human, bovine, ovine, rabbit, and rhesus monkey . Recombinant expression allows for the production of large quantities of the enzyme, facilitating detailed structural and functional analyses.

Recent studies have focused on elucidating the catalytic mechanism of GLYAT and its involvement in metabolic diseases and cancer . The enzyme’s role in glycine conjugation has gained more attention due to the excessive use of products such as benzoate (as a preservative) and common drugs like aspirin . Understanding GLYAT’s function and regulation can provide insights into its potential as a therapeutic target for various diseases.