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Glycosylated
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. In biology (but not always in chemistry), glycosylation usually refers to an enzyme-catalysed reaction, whereas glycation (also 'non-enzymatic glycation' and 'non-enzymatic glycosylation') may refer to a non-enzymatic reaction. Glycosylation is a form of co-translational and post-translational modification. Glycans serve a variety of structural and functional roles in membrane and secreted proteins. The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation. Glycosylation is also present in the cytoplasm and nucleus as the ''O''-GlcNAc modification. Aglycosylation is a feature of engineered antibodies to bypass glycosylation. Five classes of glycans are produced: * ''N''-linked glycans attached to a nitrogen of asparagi ...
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Oligosaccharide
An oligosaccharide (; ) is a carbohydrate, saccharide polymer containing a small number (typically three to ten) of monosaccharides (simple sugars). Oligosaccharides can have many functions including Cell–cell recognition, cell recognition and cell adhesion. They are normally present as glycans: oligosaccharide chains are linked to lipids or to compatible amino acid side chains in proteins, by ''N''- or ''O''-glycoside, glycosidic bonds. ''N''-Linked oligosaccharides are always pentasaccharides attached to asparagine via a beta linkage to the amine nitrogen of the side chain.. Alternately, O-linked glycosylation, ''O''-linked oligosaccharides are generally attached to threonine or serine on the alcohol group of the side chain. Not all natural oligosaccharides occur as components of glycoproteins or glycolipids. Some, such as the raffinose series, occur as storage or transport carbohydrates in plants. Others, such as maltodextrins or cellodextrins, result from the microbial break ...
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O-GlcNAc
''O''-GlcNAc (short for ''O''-linked GlcNAc or ''O''-linked β-''N''-acetylglucosamine) is a reversible Enzyme, enzymatic post-translational modification that is found on serine and threonine residues of Cell nucleus, nucleoCytoplasm, cytoplasmic proteins. The modification is characterized by a Glycosidic bond, β-glycosidic bond between the Hydroxy group, hydroxyl group of serine or threonine side chains and N-Acetylglucosamine, ''N''-acetylglucosamine (GlcNAc). ''O''-GlcNAc differs from other forms of protein glycosylation: (i) ''O''-GlcNAc is not elongated or modified to form more complex glycan structures, (ii) ''O''-GlcNAc is almost exclusively found on nuclear and cytoplasmic proteins rather than membrane proteins and secretory proteins, and (iii) ''O''-GlcNAc is a highly dynamic modification that turns over more rapidly than the proteins which it modifies. ''O''-GlcNAc is conserved across Animal, metazoans. Due to the dynamic nature of ''O''-GlcNAc and its presence on seri ...
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Lipid
Lipids are a broad group of organic compounds which include fats, waxes, sterols, fat-soluble vitamins (such as vitamins A, D, E and K), monoglycerides, diglycerides, phospholipids, and others. The functions of lipids include storing energy, signaling, and acting as structural components of cell membranes. Lipids have applications in the cosmetic and food industries, and in nanotechnology. Lipids are broadly defined as hydrophobic or amphiphilic small molecules; the amphiphilic nature of some lipids allows them to form structures such as vesicles, multilamellar/ unilamellar liposomes, or membranes in an aqueous environment. Biological lipids originate entirely or in part from two distinct types of biochemical subunits or "building-blocks": ketoacyl and isoprene groups. Using this approach, lipids may be divided into eight categories: fatty acyls, glycerolipids, glycerophospholipids, sphingolipids, saccharolipids, and polyketides (derived from condensatio ...
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Glycoconjugate
In molecular biology and biochemistry, glycoconjugates are the classification family for carbohydrates – referred to as glycans – which are covalently linked with chemical species such as proteins, peptides, lipids, and other compounds. Glycoconjugates are formed in processes termed glycosylation. Glycoconjugates are very important compounds in biology and consist of many different categories such as glycoproteins, glycopeptides, peptidoglycans, glycolipids, glycosides, and lipopolysaccharides. They are involved in cell–cell interactions, including cell–cell recognition; in cell–matrix interactions; and in detoxification processes. Generally, the carbohydrate part(s) play an integral role in the function of a glycoconjugate; prominent examples of this are neural cell adhesion molecule (NCAM) and blood proteins where fine details in the carbohydrate structure determine cell binding (or not) or lifetime in circulation. Although the important molecular species DNA, ...
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N-linked Glycosylation
''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 (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called ''N''-glycosylation, studied in biochemistry. The resulting protein is called an N-linked glycan, or simply an N-glycan. This type of linkage is important for both the structure and function of many eukaryotic proteins. The ''N''-linked glycosylation process occurs in eukaryotes and widely in archaea, but very rarely in bacteria. The nature of ''N''-linked glycans attached to a glycoprotein is determined by the protein and the cell in which it is expressed. It also varies across species. Different species synthesize different types of ''N''-linked glycans. Energetics of bond formation There are two types of bonds involved in a glycoprotein: bonds between the saccharides residues in the glycan and the linkage between ...
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Tyrosine
-Tyrosine or tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a conditionally essential amino acid with a polar side group. The word "tyrosine" is from the Greek ''tyrós'', meaning ''cheese'', as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. It is called tyrosyl when referred to as a functional group or side chain. While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is encoded by the codons UAC and UAU in messenger RNA. The one-letter symbol Y was assigned to tyrosine for being alphabetically nearest of those letters available. Note that T was assigned to the structurally simpler threonine, U was avoided for its similarity with V for valine, W was assigned to tryptophan, while X was reserved for undetermined or atypical amino acids. The mnemonic t''Y''rosine was ...
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Hydroxylysine
Hydroxylysine (Hyl) is an amino acid with the molecular formula C6H14N2O3. It was first discovered in 1921 by Donald Van Slyke as the 5-hydroxylysine form. It arises from a post-translational hydroxy modification of lysine. It is most widely known as a component of collagen Collagen () is the main structural protein in the extracellular matrix of the connective tissues of many animals. It is the most abundant protein in mammals, making up 25% to 35% of protein content. Amino acids are bound together to form a trip .... It is biosynthesized from lysine via oxidation by lysyl hydroxylase enzymes. The most common form is the (5''R'') stereoisomer found in collagen. However, the enzyme JMJD6 has recently been shown to be a lysyl hydroxylase which modifies an RNA splicing factor producing the (5''S'') stereoisomer. Additionally, in ''E. coli'', there has been at least one lysine ''N''-hydroxylase enzyme identified, named IucD. References External links * {{MeshName, Hydrox ...
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Hydroxyproline
(2''S'',4''R'')-4-Hydroxyproline, or L-hydroxyproline ( C5 H9 O3 N), is an amino acid, abbreviated as Hyp or O, ''e.g.'', in Protein Data Bank. Structure and discovery In 1902, Hermann Emil Fischer isolated hydroxyproline from hydrolyzed gelatin. In 1905, Hermann Leuchs synthesized a racemic mixture of 4-hydroxyproline. Hydroxyproline differs from proline by the presence of a hydroxyl (OH) group attached to the gamma carbon atom. Production and function Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl 4-hydroxylase following protein synthesis (as a post-translational modification). The enzyme-catalyzed reaction takes place in the lumen of the endoplasmic reticulum. Although it is not directly incorporated into proteins, hydroxyproline comprises roughly 4% of all amino acids found in animal tissue, an amount greater than seven other amino acids that are translationally incorporated. Animals Collagen Hydroxyproline is a ...
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Ceramide
Ceramides are a family of waxy lipid molecules. A ceramide is composed of sphingosine and a fatty acid joined by an amide bond. Ceramides are found in high concentrations within the cell membrane of Eukaryote, eukaryotic cells, since they are component lipids that make up sphingomyelin, one of the major lipids in the lipid bilayer. Contrary to previous assumptions that ceramides and other sphingolipids found in cell membrane were purely supporting structural elements, ceramide can participate in a variety of cellular lipid signaling, signaling: examples include regulating cell differentiation, differentiation, cell proliferation, proliferation, and programmed cell death (PCD) of Cell (biology), cells. The word ''ceramide'' comes from the Latin ''cera'' (wax) and ''amide''. Ceramide is a component of vernix caseosa, the waxy or cheese-like white substance found coating the skin of newborn human infants. Pathways for ceramide synthesis There are three major pathways of ceramide ...
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Aloin
Aloin, also known as barbaloin, is a bitter, yellow-brown colored compound noted in the exudate of at least 68 ''Aloe'' species at levels from 0.1 to 6.6% of leaf dry weight (making between 3% and 35% of the total exudate), and in another 17 species at indeterminate levels eynolds, 1995b It is used as a stimulant-laxative, treating constipation by inducing bowel movements. The compound is present in what is commonly referred to as the aloe latex that exudes from cells adjacent to the vascular bundles, found under the rind of the leaf and in between it and the gel. When dried, it has been used as a bittering agent in commerce (alcoholic beverages) 1 CFR 172.510. Scientific names given include ''Aloe perryi'', ''A. barbadensis'' (= ''A. vera''), ''A. ferox'', and hybrids of ''A. ferox'' with ''A. africana'' and ''A. spicata''. Aloe is listed in federal regulations as a natural substance that may be "safely used in food" when used "in the minimum quantity required to produce their i ...
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Tryptophan
Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent. Tryptophan is also a precursor to the neurotransmitter serotonin, the hormone melatonin, and vitamin B3 (niacin). It is encoded by the codon UGG. Like other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (–; pKa = 9.39) and the carboxylic acid is deprotonated ( –COO−; pKa = 2.38). Humans and many animals cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid. Tryptophan is named after the digestive enzymes trypsin, which were used in its first isolation from casein proteins. It was assigned the one-letter symbol W based on the double ring being visually suggestive to the bulky letter. Function ...
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Serine
Serine (symbol Ser or S) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α- amino group (which is in the protonated − form under biological conditions), a carboxyl group (which is in the deprotonated − form under biological conditions), and a side chain consisting of a hydroxymethyl group, classifying it as a polar amino acid. It can be synthesized in the human body under normal physiological circumstances, making it a nonessential amino acid. It is encoded by the codons UCU, UCC, UCA, UCG, AGU and AGC. Occurrence This compound is one of the proteinogenic amino acids. Only the L- stereoisomer appears naturally in proteins. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865 by Emil Cramer. Its name is derived from the Latin for silk, '' sericum''. Serine's structure was established in ...
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