α-1,2-fucosyltransferase
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α-1,2-fucosyltransferase
In enzymology, a galactoside 2-alpha-L-fucosyltransferase () is an enzyme that catalysis, catalyzes the chemical reaction :GDP-beta-L-fucose + beta-D-galactosyl-R \rightleftharpoons GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R Thus, the two substrate (biochemistry), substrates of this enzyme are GDP-beta-L-fucose and beta-D-galactosyl-R, whereas its two product (chemistry), products are guanosine diphosphate, GDP and alpha-L-fucosyl-1,2-beta-D-galactosyl-R. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. This enzyme participates in 4 metabolism, metabolic pathways: glycosphingolipid biosynthesis - lactoseries, glycosphingolipid biosynthesis - neo-lactoseries, glycosphingolipid biosynthesis - globoseries, and glycan structures - biosynthesis 2. Nomenclature The List of enzymes, systematic name of this enzyme class is: * GDP-beta-L-fucose:beta-D-galactosyl-R 2-alpha-L-fucosyltransferase Other names in common use include: * blood ...
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Enzymology
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ...
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