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Sequence-based classification methods have proven to be a powerful way of generating hypotheses for protein function based on sequence alignment to related proteins. The carbohydrate-active enzyme database presents a sequence-based classification of glycosyltransferases into over 90 families. [10]
The process of glycosylation (binding a carbohydrate to a protein) is a post-translational modification, meaning it happens after the production of the protein. [3] Glycosylation is a process that roughly half of all human proteins undergo and heavily influences the properties and functions of the protein. [ 3 ]
Protein domains allow protein classification by a combination of sequence, structure and function, and they can be combined in many ways. In an early study of 170,000 proteins, about two-thirds were assigned at least one domain, with larger proteins containing more domains (e.g. proteins larger than 600 amino acids having an average of more ...
The human genome, categorized by function of each gene product, given both as number of genes and as percentage of all genes. [7] Proteins may also be classified based on their cellular function. A widely used classification is PANTHER (protein analysis through evolutionary relationships) classification system. [7]
Glycogen synthase (UDP-glucose-glycogen glucosyltransferase) is a key enzyme in glycogenesis, the conversion of glucose into glycogen. It is a glycosyltransferase ( EC 2.4.1.11 ) that catalyses the reaction of UDP-glucose and (1,4- α - D -glucosyl) n to yield UDP and (1,4- α - D -glucosyl) n+1 .
Sequence-based classifications are one of the most powerful predictive methods for suggesting function for newly sequenced enzymes for which function has not been biochemically demonstrated. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of more than 100 different families.
They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in fat cells. [5] Proteins can be broken down by enzymes known as peptidases or can break down as a result of denaturation. Proteins can denature in environmental conditions the protein is not made for. [6]
The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s). [2] The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate - GlcA - Gal -Gal- Xyl -PROTEIN).