Glycine Amidinotransferase

Glycine amidinotransferase should be considered a glycosylation enzyme that has a wide range of applications in pharmaceuticals. It was discovered in 1933 by Glenn Theodore Watson, and since then enzymes of this class have not undergone significant changes or improvements. In 2006, the study of the structure of the complete glycoprotein of glycine amidine transaminase was completed, including amino acids (glycine, amide and tyrosine), two subunits of E. coli (prepolymer and polypeptide), α-amino acid residues and well

Glycine amidinotransferase (Glycine-AT) is also called Glycinamide carbon transferase. Glycine-AT is located in the plasma membrane of the nuclei of epithelial cells of the pancreas, salivary glands and cerebellar cells, as well as in the smooth muscle cells of the uterus and their nerve endings.

Glycine belongs to a group of simple organic molecules that are components of proteins in living organisms. Glycine is structurally related to the amino acid serine. Increased levels of glycine (or its metabolites) in the blood serum are observed in conditions such as liver cirrhosis, shock after major burns and proteinemia. Other causes of elevated glycine levels include schizophrenia, diffuse renal malacia, neuroendocrine tumors, renal failure, hyperparathyroidism, and drug overdose.

Reduced serum glycine levels, i.e. hypoglycinemia,