Guanosine 5′-diphosphoglucose (GDP-Glucose) is a nucleotide sugar donor substrate for glucosylation reactions mediated by enzymes called glucosyltransferases. GDP-Glucose provides a source of enzyme-available glucose residues for attachment to a wide range of polysaccharide structures.
The glycogen synthase found in Pyrococcus furiosus is a hyperthermophilic biocatalyst that transfers the glucose portion of nucleotide-diphosphoglucose onto a growing carbohydrate biopolymer chain at 80 degrees C. In contrast to the mesophilic rabbit muscle glycogen synthase, the biocatalyst from
Journal of bacteriology, 189(5), 1648-1654 (2006-12-26)
The pathway for the synthesis of glucosylglycerate (GG) in the thermophilic bacterium Persephonella marina is proposed based on the activities of recombinant glucosyl-3-phosphoglycerate (GPG) synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP). The sequences of gpgS and gpgP from the cold-adapted bacterium
Proceedings of the National Academy of Sciences of the United States of America, 102(6), 2221-2226 (2005-01-14)
Glucuronoarabinoxylan, xyloglucan, and galactomannan are noncellulosic polysaccharides found in plant cell walls. All consist of beta-linked glycan backbones substituted with sugar side chains. Although considerable progress has been made in characterizing the structure of these polysaccharides, little is known about
Biochimica et biophysica acta, 1790(5), 368-374 (2009-03-18)
Purified trehalose-6-phosphate synthase (TPS) of Saccharomyces cerevisiae was effective over a wide range of substrates, although differing with regard to their relative activity. Polyanions heparin and chondroitin sulfate were seen to stimulate TPS activity, particularly when a pyrimidine glucose nucleotide
Nucleotide sugar transporters (NSTs) play an essential role in translocating nucleotide sugars into the lumen of the endoplasmic reticulum and Golgi apparatus to be used as substrates in glycosylation reactions. This intracellular transport is an essential step in the biosynthesis
Enzymatic glycosyltransferase specificity challenges the one enzyme-one linkage concept.
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