What is glycosylation? Glycosylated peptide production process

Glycosylation

Glycosylation is a process in which proteins or lipids attach glycogen under the control of enzymes, which is produced in the endoplasmic reticulum. Under the function of glycosyltransferase, sugar is transferred to protein, and glucoside bond is formed with amino acid residues on protein. Proteins undergo glycosylation to produce glycoproteins. Glycosylation is the key decorative function of protein, which has the function of regulating protein.

process

The formation of N-linked sugar chain originates from endoplasmic reticulum and proceeds from Golgi. The glycoproteins produced by endoplasmic reticulum (ER) have similar sugar chains. After entering Golgi bodies from CIS surface, a series of orderly production, processing and decoration took place in the middle of each membrane capsule. Most of the mannose in the original sugar chain was removed, but different kinds of sugar molecular structures were added by various glycosyltransferases, resulting in different structures of oligosaccharides Chain. The spatial structure of glycoprotein determines which glycosyltransferase it can fuse with to produce special glycosylation decoration.

Many glycoproteins also have N-linked and O-linked sugar chains. The glycosylation of o-junction is carried out in Golgi matrix. Generally, the first linked sugar module is n-acetylgalactose, which is linked to the methyl groups of SER, thr and hyp. Then, the glycosyl groups are transferred to the Golgi matrix to form oligosaccharide chains. The kidney source of glucose is nucleoside sugar, such as UDP galactose. As a result of glycosylation, different proteins are labeled differently, which changes the conformation of polypeptides and improves the reliability of proteins. In Golgi apparatus, one to several amino glycan chains can be installed on serine residues of key proteins according to xylose to produce proteoglycan. Some of these proteins are metabolized outside the somatic cells to produce extracellular matrix or mucus layer, and some are directed to the membrane.

classification

According to the types of glycoside chains, protein glycosylation can be divided into four types, namely, the methyl groups of serine, threonine, hydroxylysine and hydroxyproline are used as nodes to produce - 0-glycosidic bond. The amino group of asparagine, the α - amino group of N-terminal amino acid and the ω - amino group of lysine or arginine are used as nodes to produce - N-glycosidic bond; the dispersed carboxyl group of aspartic acid or glutamic acid is used as the node to produce the lipoglycoside bond and the glycopeptide bond with cysteine as the node.

At the end:

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