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The kinase enzymes increase the rate of the reactions by making the inositol hydroxyl group more nucleophilic, often using the side chain of an amino acid residue to act as a general base and deprotonate the hydroxyl, as seen in the mechanism below. [24] Here, a reaction between adenosine triphosphate (ATP) and phosphatidylinositol is coordinated.
An endoenzyme, or intracellular enzyme, is an enzyme that functions within the cell in which it was produced. [1] Because the majority of enzymes fall within this category, the term is used primarily to differentiate a specific enzyme from an exoenzyme. It is possible for a single enzyme to have both endoenzymatic and exoenzymatic functions ...
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...
Above is a ball-and-stick model of the inorganic phosphate molecule (H PO 4 2−).Colour coding: P (orange); O (red); H (white). The chemical activity of a protein kinase involves removing a phosphate group from ATP and covalently attaching it to one of three amino acids that have a free hydroxyl group.
Ribbon representation of the Streptomyces lividans β-1,4-endoglucanase catalytic domain - an example from the family 12 glycoside hydrolases [1]. Cellulase (EC 3.2.1.4; systematic name 4-β-D-glucan 4-glucanohydrolase) is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides:
β-Amylase (EC 3.2.1.2, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. [ 2 ] [ 3 ] [ 4 ] It catalyses the following reaction: Hydrolysis of (1→4)-α- D -glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids.It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common.
Glycosylation is the reaction in which a carbohydrate (or 'glycan'), i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor) in order to form a glycoconjugate.