GLYATL2 Human
Description
Product Specs
Product Science Overview
Glycine-N-Acyltransferase-Like 2 (GLYATL2) is a protein encoded by the GLYATL2 gene in humans. This enzyme is part of a family of glycine conjugating enzymes that play a crucial role in the metabolism of fatty acids and other bioactive lipids. The recombinant form of this enzyme is produced through biotechnological methods to study its function and potential applications in various fields, including biochemistry and pharmacology.
The GLYATL2 gene is located on chromosome 11 and is responsible for encoding the Glycine-N-Acyltransferase-Like 2 protein. This protein is a mitochondrial acyltransferase that transfers acyl groups to the N-terminus of glycine. The enzyme is involved in the conjugation of various substrates, such as arachidonoyl-CoA and saturated medium and long-chain acyl-CoAs, to form a variety of N-acyl glycines .
GLYATL2 exhibits glycine N-acyltransferase activity, which is essential for the catabolism of long-chain and medium-chain fatty acids. The enzyme preferentially conjugates monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor. It does not exhibit activity toward certain substrates like C22:6-CoA and chenodeoxycholoyl-CoA, nor toward amino acids such as serine or alanine .
The biological activities of N-acyl glycines, the products of GLYATL2 activity, include antinociceptive (pain-relieving), anti-inflammatory, and antiproliferative effects. These compounds also activate G-protein-coupled receptors, contributing to their role as bioactive lipids .
The GLYATL2 enzyme is localized to the endoplasmic reticulum. Its mRNA shows the highest expression in the salivary gland and trachea, but it is also detected in the spinal cord and skin fibroblasts. This expression pattern suggests a role for N-acyl glycines in barrier function and immune response .
The recombinant form of GLYATL2 is used in research to understand its function and potential therapeutic applications. Studies have shown that recombinantly expressed GLYATL2 efficiently conjugates oleoyl-CoA, arachidonoyl-CoA, and other medium- and long-chain acyl-CoAs to glycine. This specificity for glycine as an acceptor molecule and the preferential production of N-oleoyl glycine highlight its importance in lipid metabolism .
