Related Research Articles
In biochemistry, a transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups from one molecule to another. They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes.
Glycolipids are lipids with a carbohydrate attached by a glycosidic (covalent) bond. Their role is to maintain the stability of the cell membrane and to facilitate cellular recognition, which is crucial to the immune response and in the connections that allow cells to connect to one another to form tissues. Glycolipids are found on the surface of all eukaryotic cell membranes, where they extend from the phospholipid bilayer into the extracellular environment.
Oligosaccharyltransferase or OST (EC 2.4.1.119) is a membrane protein complex that transfers a 14-sugar oligosaccharide from dolichol to nascent protein. It is a type of glycosyltransferase. The sugar Glc3Man9GlcNAc2 (where Glc=Glucose, Man=Mannose, and GlcNAc=N-acetylglucosamine) is attached to an asparagine (Asn) residue in the sequence Asn-X-Ser or Asn-X-Thr where X is any amino acid except proline. This sequence is called a glycosylation sequon. The reaction catalyzed by OST is the central step in the N-linked glycosylation pathway.
1,4-alpha-glucan-branching enzyme, also known as brancher enzyme or glycogen-branching enzyme is an enzyme that in humans is encoded by the GBE1 gene.
Glycosyltransferases are enzymes that establish natural glycosidic linkages. They catalyze the transfer of saccharide moieties from an activated nucleotide sugar to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur-based.
Xyloglucan is a hemicellulose that occurs in the primary cell wall of all vascular plants; however, all enzymes responsible for xyloglucan metabolism are found in Charophyceae algae. In many dicotyledonous plants, it is the most abundant hemicellulose in the primary cell wall. Xyloglucan binds to the surface of cellulose microfibrils and may link them together. It is the substrate of xyloglucan endotransglycosylase, which cuts and ligates xyloglucans, as a means of integrating new xyloglucans into the cell wall. It is also thought to be the substrate of alpha-expansin, which promotes cell wall enlargement.
Brassinolide is a plant hormone. The first isolated brassinosteroid, it was discovered when it was shown that pollen from rapeseed could promote stem elongation and cell division. The biologically active component was isolated and named brassinolide.
The enzyme mannosyl-glycoprotein endo-β-N-acetylglucosaminidase (endoglycosidase H) (EC 3.2.1.96) has systematic name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase. It is a highly specific endoglycosidase which cleaves asparagine-linked mannose rich oligosaccharides, but not highly processed complex oligosaccharides from glycoproteins. It is used for research purposes to deglycosylate glycoproteins and to monitor intracellular protein trafficking through the secretory pathway.
Galactosyltransferase is a type of glycosyltransferase which catalyzes the transfer of galactose. An example is B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase.
Nucleotide sugars are the activated forms of monosaccharides. Nucleotide sugars act as glycosyl donors in glycosylation reactions. Those reactions are catalyzed by a group of enzymes called glycosyltransferases.
In enzymology, a xyloglucan-specific endo-beta-1,4-glucanase (EC 3.2.1.151) is an enzyme that catalyzes the chemical reaction
In enzymology, a beta-galactoside alpha-2,6-sialyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a 4-alpha-glucanotransferase is an enzyme that catalyzes a chemical reaction that transfers a segment of a 1,4-alpha-D-glucan to a new position in an acceptor carbohydrate, which may be glucose or a 1,4-alpha-D-glucan.
In enzymology, a cyclomaltodextrin glucanotransferase is an enzyme that catalyzes the chemical reaction of cyclizing part of a 1,4-alpha-D-glucan molecule through the formation of a 1,4-alpha-D-glucosidic bond. They are bacterial enzymes belonging to the same family of the α-amylase specifically known as glycosyl-hydrolase family 13. This peculiar enzyme is capable of catalyzing more than one reaction with the most important being the synthesis of non-reducing cyclic dextrins known as cyclodextrins starting from starch, amylose, and other polysaccharides.
In enzymology, a xyloglucan 4-glucosyltransferase is an enzyme that catalyzes the chemical reaction in which a beta-D-glucosyl residue is transferred from UDP-glucose to another glucose residue in xyloglucan, linked by a beta-1,4-D-glucosyl-D-glucose bond.
In enzymology, a xyloglucan 6-xylosyltransferase is an enzyme that catalyzes the chemical reaction in which an alpha-D-xylosyl residue is transferred from UDP-D-xylose to a glucose residue in xyloglucan, being attached by an alpha-1,6-D-xylosyl-D-glucose bond.
Histo-blood group ABO system transferase is an enzyme with glycosyltransferase activity, which is encoded by the ABO gene in humans. It is ubiquitously expressed in many tissues and cell types. ABO determines the ABO blood group of an individual by modifying the oligosaccharides on cell surface glycoproteins. Variations in the sequence of the protein between individuals determine the type of modification and the blood group. The ABO gene also contains one of 27 SNPs associated with increased risk of coronary artery disease.
N-linked glycosylation, is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom, in a process called N-glycosylation, studied in biochemistry. The resulting protein is called an N-linked glycan, or simply an N-glycan.
Mixed-linkage glucan : xyloglucan endotransglucosylase (MXE) is a plant cell wall-modifying enzyme found in plants of the genus Equisetum. The enzyme is proposed, in vivo, to catalyse the endotransglucosylation of two different hemicellulose polysaccharides, mixed-linkage glucan and xyloglucan, effectively 'stitching' them together. However only the 'stitching' of a mixed-linkage glucan polysaccharide to a xyloglucan oligosaccharide has actually been witnessed to date.
Glucanases are enzymes that break down large polysaccharides via hydrolysis. The product of the hydrolysis reaction is called a glucan, a linear polysaccharide made of up to 1200 glucose monomers, held together with glycosidic bonds. Glucans are abundant in the endosperm cell walls of cereals such as barley, rye, sorghum, rice, and wheat. Glucanases are also referred to as lichenases, hydrolases, glycosidases, glycosyl hydrolases, and/or laminarinases. Many types of glucanases share similar amino acid sequences but vastly different substrates. Of the known endo-glucanases, 1,3-1,4-β-glucanase is considered the most active.
References
- ↑ Thompson, James E.; Fry, Stephen C. (2001). "Restructuring of wall-bound xyloglucan by transglycosylation in living plant cells" (PDF). The Plant Journal. 26 (1): 23–34. doi: 10.1046/j.1365-313x.2001.01005.x . PMID 11359607.
- Fry SC, Smith RC, Renwick KF, Martin DJ, Hodge SK, Matthews KJ (1992). "Xyloglucan endotransglycosylase, a new wall-loosening enzyme activity from plants". Biochem. J. 282 (Pt 3): 821–8. doi:10.1042/bj2820821. PMC 1130861 . PMID 1554366.
- Nishitani K, Tominaga R (1992). "Endo-xyloglucan transferase, a novel class of glycosyltransferase that catalyzes transfer of a segment of xyloglucan molecule to another xyloglucan molecule". J. Biol. Chem. 267 (29): 21058–64. PMID 1400418.
- Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM (2006). "A proteomic analysis of arsenical drug resistance in Trypanosoma brucei". Proteomics. 6 (9): 2726–32. doi:10.1002/pmic.200500419. PMID 16526094. S2CID 24074942.
- Lorences EP, Fry, SC (1993). "Xyloglucan oligosaccharides with at least two alpha-D-xylose residues act as acceptor substrates for xyloglucan endotransglycosylase and promote the depolymerisation of xyloglucan". Plant Physiol. 88: 105–112. doi:10.1111/j.1399-3054.1993.tb01767.x.
