GlucosamineSulfuric Acids: Inorganic and organic derivatives of sulfuric acid (H2SO4). The salts and esters of sulfuric acid are known as SULFATES and SULFURIC ACID ESTERS respectively.Tamarindus: A plant genus of the family FABACEAE known for its sour fruit.Acetylglucosamine: The N-acetyl derivative of glucosamine.Datura stramonium: A plant species of the genus DATURA, family SOLANACEAE, that contains TROPANES and other SOLANACEOUS ALKALOIDS.Herbaspirillum: A genus of gram-negative bacteria in the family OXALOBACTERACEAE, comprised of vibrioid or sometimes helical cells. They are chemoorganotrophic nitrogen fixers and are found free-living in the soil or in association with the roots of members of the GRAMINEAE. (From Bergey's Manual of Determinative Bacteriology, 9th ed)Plant Lectins: Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.Osteoarthritis, Knee: Noninflammatory degenerative disease of the knee joint consisting of three large categories: conditions that block normal synchronous movement, conditions that produce abnormal pathways of motion, and conditions that cause stress concentration resulting in changes to articular cartilage. (Crenshaw, Campbell's Operative Orthopaedics, 8th ed, p2019)Chondroitin Sulfates: Derivatives of chondroitin which have a sulfate moiety esterified to the galactosamine moiety of chondroitin. Chondroitin sulfate A, or chondroitin 4-sulfate, and chondroitin sulfate C, or chondroitin 6-sulfate, have the sulfate esterified in the 4- and 6-positions, respectively. Chondroitin sulfate B (beta heparin; DERMATAN SULFATE) is a misnomer and this compound is not a true chondroitin sulfate.Osteoarthritis: A progressive, degenerative joint disease, the most common form of arthritis, especially in older persons. The disease is thought to result not from the aging process but from biochemical changes and biomechanical stresses affecting articular cartilage. In the foreign literature it is often called osteoarthrosis deformans.Neodymium: Neodymium. An element of the rare earth family of metals. It has the atomic symbol Nd, atomic number 60, and atomic weight 144.24, and is used in industrial applications.Diagnosis, Oral: Examination of the mouth and teeth toward the identification and diagnosis of intraoral disease or manifestation of non-oral conditions.Biological Products: Complex pharmaceutical substances, preparations, or matter derived from organisms usually obtained by biological methods or assay.Chitin: A linear polysaccharide of beta-1->4 linked units of ACETYLGLUCOSAMINE. It is the second most abundant biopolymer on earth, found especially in INSECTS and FUNGI. When deacetylated it is called CHITOSAN.Periodontics: A dental specialty concerned with the histology, physiology, and pathology of the tissues that support, attach, and surround the teeth, and of the treatment and prevention of disease affecting these tissues.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Hyaluronic Acid: A natural high-viscosity mucopolysaccharide with alternating beta (1-3) glucuronide and beta (1-4) glucosaminidic bonds. It is found in the UMBILICAL CORD, in VITREOUS BODY and in SYNOVIAL FLUID. A high urinary level is found in PROGERIA.Monosaccharides: Simple sugars, carbohydrates which cannot be decomposed by hydrolysis. They are colorless crystalline substances with a sweet taste and have the same general formula CnH2nOn. (From Dorland, 28th ed)Carbohydrate Sequence: The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.Uridine Diphosphate N-Acetylglucosamine: Serves as the biological precursor of insect chitin, of muramic acid in bacterial cell walls, and of sialic acids in mammalian glycoproteins.Uridine Diphosphate SugarsMuramic Acids: Compounds consisting of glucosamine and lactate joined by an ether linkage. They occur naturally as N-acetyl derivatives in peptidoglycan, the characteristic polysaccharide composing bacterial cell walls. (From Dorland, 28th ed)Uridine Diphosphate: A uracil nucleotide containing a pyrophosphate group esterified to C5 of the sugar moiety.Uridine Diphosphate Glucose: A key intermediate in carbohydrate metabolism. Serves as a precursor of glycogen, can be metabolized into UDPgalactose and UDPglucuronic acid which can then be incorporated into polysaccharides as galactose and glucuronic acid. Also serves as a precursor of sucrose lipopolysaccharides, and glycosphingolipids.Glucuronosyltransferase: A family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines, and fatty acids. They function as drug-metabolizing enzymes that catalyze the conjugation of UDPglucuronic acid to a variety of endogenous and exogenous compounds. EC 2.4.1.17.Cell Wall: The outermost layer of a cell in most PLANTS; BACTERIA; FUNGI; and ALGAE. The cell wall is usually a rigid structure that lies external to the CELL MEMBRANE, and provides a protective barrier against physical or chemical agents.Uracil NucleotidesTransferases (Other Substituted Phosphate Groups): A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.Tunicamycin: An N-acetylglycosamine containing antiviral antibiotic obtained from Streptomyces lysosuperificus. It is also active against some bacteria and fungi, because it inhibits the glucosylation of proteins. Tunicamycin is used as tool in the study of microbial biosynthetic mechanisms.Phosphotransferases: A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Phosphates: Inorganic salts of phosphoric acid.SulfatasesMucolipidoses: A group of inherited metabolic diseases characterized by the accumulation of excessive amounts of acid mucopolysaccharides, sphingolipids, and/or glycolipids in visceral and mesenchymal cells. Abnormal amounts of sphingolipids or glycolipids are present in neural tissue. INTELLECTUAL DISABILITY and skeletal changes, most notably dysostosis multiplex, occur frequently. (From Joynt, Clinical Neurology, 1992, Ch56, pp36-7)

Crystal structures of two H-2Db/glycopeptide complexes suggest a molecular basis for CTL cross-reactivity. (1/1610)

Two synthetic O-GlcNAc-bearing peptides that elicit H-2Db-restricted glycopeptide-specific cytotoxic T cells (CTL) have been shown to display nonreciprocal patterns of cross-reactivity. Here, we present the crystal structures of the H-2Db glycopeptide complexes to 2.85 A resolution or better. In both cases, the glycan is solvent exposed and available for direct recognition by the T cell receptor (TCR). We have modeled the complex formed between the MHC-glycopeptide complexes and their respective TCRs, showing that a single saccharide residue can be accommodated in the standard TCR-MHC geometry. The models also reveal a possible molecular basis for the observed cross-reactivity patterns of the CTL clones, which appear to be influenced by the length of the CDR3 loop and the nature of the immunizing ligand.  (+info)

Gangliosides of human kidney. (2/1610)

Five gangliosides isolated from human kidney have been characterized. The two main fractions were shown to be typical extraneural gangliosides in having lactose as their neutral carbohydrate moiety. Their structures were identified as: AcNeu(alpha2-3)Gal(beta1-4)Glc(beta1-1)Cer and AcNeu(alpha2-8)AcNeu(alpha2-3)Gal(beta1-4)Glc(beta1-1)Cer. The two main hexosamine-containing gangliosides are structurally related to human blood group substances of glycosphingolipid nature. The following structures are postulated: AcNeu(alpha2-3)Gal(beta1-4)GlcNAc(beta1-3)Gal(beta1-4)Glc(beta1-1)Cer and AcNeu(alpha2-3)Gal(beta1-4)[Fuc(alpha1-3)]GlcNAc(beta1-3)Gal(beta1-4)Glc(beta1-1) Cer. The third hexosamine-containing ganglioside belongs to a different series of glycolipids and was shown to have the structure of a major ganglioside of human brain: AcNeu(alpha2-3)Gal(beta1-3)GalNAc(beta1-4)[AcNeu(alpha2-3)]Gal(beta1-4)Glc(beta1- 1)Cer. The fatty acid structure of different gangliosides was shown to resemble that of neutral glycolipids of human kidney with the nonhydroxy acids C16:0, C22:0, and C24:0 as major components.  (+info)

Participation of a trisaccharide-lipid in glycosylation of oviduct membrane glycoproteins. (3/1610)

Preincubation of a hen oviduct membrane preparation with UDP-Nactyl[14C]glucosamine and bacitracin, followed by incubation with GDP-mannose, leads to formation of a chloroform/methanol (2/1)-extractable glycolipid. Treatment of the lipid with mild acid results in the release of a trisaccharide shown to have the structure beta-mannosyl-N-acetylglucosamineyl-N-acetylglucosamine. Incubation of purified trisaccharide-lipid with oviduct membranes in the presence of sodium deoxycholate, Mn2+, and GDP-mannose leads to formation of a labeled glycoprotein with an apparent molecular weight of 25,000...  (+info)

Lectin receptor sites on rat liver cell nuclear membranes. (4/1610)

The presence and localization of lectin receptor sites on rat liver cell nuclear and other endomembranes was studied by light and electron microscopy using fluorescein and ferritin-coupled lectin conjugates. Isolated nuclei labelled with fluorescein-conjugated Concanavalin A (Con A) or wheat germ agglutinin (WGA) often showed membrane staining, which sometimes was especially bright on small stretches of the nuclear surface. Unlabelled nuclei and nuclei with a complete ring fluorescence were also seen. The nuclear fluorescence corresponded in intensity to that seen on the surface of isolated rat liver cells. Con A-ferritin particles were seldom detected on the cytoplasmic surface of the intact nuclear envelope. However, at places where the 2 leaflets of the envelope were widely separated or where the outer nuclear membrane was partly torn away, heavy labelling was seen on the cisternal surface of both the inner and outer nuclear membranes. Labelling with Con A-ferritin was also found on the cisternal side of rough endoplasmic reticulum present in the specimens. No labelling was seen on the cytoplasmic surface of mitochondrial outer membrane. The results demonstrate the presence of binding sites for Con A and WGA in nuclei and an asymmetric localization of these sites on the cisternal side of ribosome-carrying endomembranes in rat liver cells.  (+info)

Role of surface proteins in Vibrio cholerae attachment to chitin. (5/1610)

The role of surface proteins in Vibrio cholerae attachment to chitin particles in vitro was studied. Treatment of V. cholerae O1 ATCC 14034 and ATCC 14035 with pronase E reduced the attachment of bacteria to chitin particles by 57 to 77%. A statistically significant reduction was also observed when the attachment to chitin was evaluated in the presence of homologous Sarkosyl-insoluble membrane proteins (MPs) (67 to 84%), N-acetylglucosamine (GlcNAc) (62%), the sugar that makes up chitin, and wheat germ agglutinin (40 to 56%), a lectin that binds GlcNAc. The soluble oligomers N,N'-diacetylchitobiose or N,N', N"-triacetylchitotriose caused an inhibition of 14 to 23%. Sarkosyl-insoluble MPs able to bind chitin particles were isolated and visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; two of these peptides (molecular sizes, 36 and 53 kDa) specifically bind GlcNAc.  (+info)

Platelet high affinity low density lipoprotein binding and import of lipoprotein derived phospholipids. (6/1610)

The binding of low density lipoprotein (LDL) to the platelet cell membrane could facilitate the transfer of phospholipids from LDL to the platelets. A polyclonal antibody against the platelet glycoproteins IIb/IIIa inhibited the high affinity binding of 125I-LDL by up to 80%. The transfer of pyrene (py)-labeled sphingomyelin (SM), phosphatidylcholine and phosphatidylethanolamine from LDL to the platelets was unaffected by the antibody. The lectin wheat germ agglutinin (WGA) reduced the binding of 125I-LDL to the platelets by approximately 80%. In contrast, the lectin stimulated the transfer of SM from LDL into the platelets by about three-fold. WGA also specifically augmented the transfer of py-SM between lipid vesicles and the platelets, the stimulation being abolished in the presence of N-acetylglucosamine. Dextran sulfate (DS) increased the specific binding of 125I-LDL to the platelets by up to 2.8-fold. On the other hand, the import of LDL-derived py-phospholipids was unaffected by DS. Together, the results indicate that the phospholipid transfer from LDL to the platelets is independent of the high affinity LDL binding to the platelets and is specifically stimulated by WGA. Thus, the interactions of platelets with LDL phospholipids differ markedly from those with the apoprotein components of the lipoproteins.  (+info)

Mutations that confer resistance to 2-deoxyglucose reduce the specific activity of hexokinase from Myxococcus xanthus. (7/1610)

The glucose analog 2-deoxyglucose (2dGlc) inhibits the growth and multicellular development of Myxococcus xanthus. Mutants of M. xanthus resistant to 2dGlc, designated hex mutants, arise at a low spontaneous frequency. Expression of the Escherichia coli glk (glucokinase) gene in M. xanthus hex mutants restores 2dGlc sensitivity, suggesting that these mutants arise upon the loss of a soluble hexokinase function that phosphorylates 2dGlc to form the toxic intermediate, 2-deoxyglucose-6-phosphate. Enzyme assays of M. xanthus extracts reveal a soluble hexokinase (ATP:D-hexose-6-phosphotransferase; EC 2.7.1.1) activity but no phosphotransferase system activities. The hex mutants have lower levels of hexokinase activities than the wild type, and the levels of hexokinase activity exhibited by the hex mutants are inversely correlated with the ability of 2dGlc to inhibit their growth and sporulation. Both 2dGlc and N-acetylglucosamine act as inhibitors of glucose turnover by the M. xanthus hexokinase in vitro, consistent with the finding that glucose and N-acetylglucosamine can antagonize the toxic effects of 2dGlc in vivo.  (+info)

Quantitative determination of N-acetylglucosamine residues at the non-reducing ends of peptidoglycan chains by enzymic attachment of [14C]-D-galactose. (8/1610)

The ability of human milk galactosyltransferase to attach D-galactose residues quantitatively to the C-4 of N-acetylglucosamine moieties at the ends of oligosaccharides has been utilized for the specific labeling and quantitative determination of the chain length of the glycan moiety of the bacterial cell wall. The average polysaccharide chain length of the soluble, uncrosslinked peptidoglycan secreted by Micrococcus luteus cells on incubation with penicillin G was studied with this technique and found to be approximately 70 hexosamines long. Furthermore, the peptidoglycan chain length of Escherichia coli sacculi of different cell shapes and dimensions was determined both in rod-shaped cells and in filaments induced by temperature shift of a division mutant or by addition of cephalexin or nalidixic acid. The average chain length found in most of these sacculi was between 70 and 100 hexosamines long. Small spherical 'mini' cells had chain lengths similar to those of the isogenic rod-like cells.  (+info)

*N-Acetylglucosamine

... (N-acetyl-D-glucosamine, or GlcNAc, or NAG) is a monosaccharide and a derivative of glucose. It is an amide ... "Inhibition of elastase enzyme release from human polymorphonuclear leukocytes by N-acetyl-galactosamine and N-acetyl-glucosamine ...

*N-acetylglucosamine deacetylase

I. N-Acetylglucosamine deacetylase". J. Biol. Chem. 226: 115-123. PMID 13428742. Molecular and Cellular Biology portal. ... In enzymology, a N-acetylglucosamine deacetylase (EC 3.5.1.33) is an enzyme that catalyzes the chemical reaction N-acetyl-D- ...

*N-acetylglucosamine kinase

In enzymology, a N-acetylglucosamine kinase (EC 2.7.1.59) is an enzyme that catalyzes the chemical reaction ATP + N-acetyl-D- ... doi:10.1016/0076-6879(66)09085-2. Datta A (1970). "Studies on hog spleen N-acetylglucosamine kinase. I. Purification and ... Other names in common use include acetylglucosamine kinase (phosphorylating), ATP:2-acetylamino-2-deoxy-D-glucose 6- ... properties of N-acetylglucosamine kinase". Biochim. Biophys. Acta. 220 (1): 51-60. doi:10.1016/0005-2744(70)90228-7. PMID ...

*N-Acetylglucosamine receptor

The N-Acetylglucosamine receptor is a receptor which binds N-Acetylglucosamine. N-Acetylglucosamine Receptor at the US National ...

*Uridine diphosphate N-acetylglucosamine

... or UDP-GlcNAc is a nucleotide sugar and a coenzyme in metabolism. It is used by ... UDP-GlcNAc is extensively involved in intracellular signaling as a substrate for O-linked N-acetylglucosamine transferases ( ... Hanover, J. A. (2001). "Glycan-dependent signaling: O-linked N-acetylglucosamine". The FASEB Journal. 15: 1865-1876. doi: ... glycosyltransferases to transfer N-acetylglucosamine residues to substrates. D-Glucosamine is made naturally in the form of ...

*N-acetylglucosamine-6-sulfatase

N-acetylglucosamine 6-sulfate sulfatase, O,N-disulfate O-sulfohydrolase, acetylglucosamine 6-sulfatase, chondroitinsulfatase, ... N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase is an enzyme that in humans is encoded by the ... N-acetylglucosamine-6-sulfatase at the US National Library of Medicine Medical Subject Headings (MeSH) This article ... Kresse H, Fuchs W, Glössl J, Holtfrerich D, Gilberg W (December 1981). "N-acetylglucosamine-6-sulfate by human β-N- ...

*Peptidoglycan-N-acetylglucosamine deacetylase

N-acetylglucosamine deacetylase, peptidoglycan GlcNAc deacetylase, peptidoglycan N-acetylglucosamine deacetylase, PG N- ... Peptidoglycan-N-acetylglucosamine deacetylase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular ... Peptidoglycan-N-acetylglucosamine deacetylase (EC 3.5.1.104, HP310, PgdA, SpPgdA, BC1960, peptidoglycan deacetylase, ... "Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis". J. Biol ...

*UDP-N-acetylglucosamine kinase

... (EC 2.7.1.176, UNAG kinase, zeta toxin, toxin PezT, ATP:UDP-N-acetyl-D-glucosamine 3'- ... UDP-N-acetylglucosamine kinase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... UDP-N-acetylglucosamine 1-carboxyvinyltransferase. These enzymes are found as part of plasmid-encoded and chromosomal bacterial ...

*UDP-N-acetylglucosamine diphosphorylase

Acetylglucosamine 1-phosphate uridylyltransferase, UDP-acetylglucosamine pyrophosphorylase, uridine diphosphate-N- ... acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine phosphorylase, and acetylglucosamine 1-phosphate ... In enzymology, an UDP-N-acetylglucosamine diphosphorylase (EC 2.7.7.23) is an enzyme that catalyzes the chemical reaction UTP ... Other names in common use include UDP-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine ...

*N-acetylglucosamine-1-phosphate transferase

... is a transferase enzyme. It is made up of two alpha (α), two beta (β), and two ... GeneReviews/NIH/NCBI/UW entry on Mucolipidosis II GeneReviews/NIH/NCBI/UW entry on Mucolipidosis III Gamma N-acetylglucosamine- ...

*UDP-N-acetylglucosamine 2-epimerase

... uridine diphospho-N-acetylglucosamine 2'-epimerase, and uridine diphosphate-N-acetylglucosamine-2'-epimerase. This enzyme ... The UDP-N-acetylglucosamine 2-epimerase from rat liver displays both epimerase and kinase activity. As of late 2007, 4 ... In enzymology, an UDP-N-acetylglucosamine 2-epimerase (EC 5.1.3.14) is an enzyme that catalyzes the chemical reaction UDP-N- ... Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase". J. Biol. Chem ...

*UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Other names in common use include MurA transferase, UDP-N-acetylglucosamine 1-carboxyvinyl-transferase, UDP-N-acetylglucosamine ... pyruvate-UDP-acetylglucosamine transferase, pyruvate-uridine diphospho-N-acetylglucosamine transferase, pyruvate-uridine ... In enzymology, an UDP-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) is an enzyme that catalyzes the chemical ... II Purification and properties of pyruvate-uridine diphospho-N-acetylglucosamine transferase and characterization of uridine ...

*N-acetylglucosamine-6-phosphate deacetylase

"Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from ... In enzymology, a N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) is an enzyme that catalyzes the chemical reaction N- ... White RJ, Pasternak CA (1967). "The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia ... Other names in common use include acetylglucosamine phosphate deacetylase, acetylaminodeoxyglucosephosphate acetylhydrolase, ...

*UDP-N-acetylglucosamine 6-dehydrogenase

In enzymology, an UDP-N-acetylglucosamine 6-dehydrogenase (EC 1.1.1.136) is an enzyme that catalyzes the chemical reaction UDP- ... Other names in common use include uridine diphosphoacetylglucosamine dehydrogenase, UDP-acetylglucosamine dehydrogenase, UDP-2- ...

*UDP-N-acetylglucosamine 4-epimerase

... uridine diphosphate N-acetylglucosamine-4-epimerase, and uridine 5'-diphospho-N-acetylglucosamine-4-epimerase. This enzyme ... In enzymology, an UDP-N-acetylglucosamine 4-epimerase (EC 5.1.3.7) is an enzyme that catalyzes the chemical reaction UDP-N- ... Other names in common use include UDP acetylglucosamine epimerase, uridine diphosphoacetylglucosamine epimerase, ...

*UDP-N-acetylglucosamine enolpyruvyl transferase

... (or MurA) is an enzyme that catalyzes the first committed step in peptidoglycan ... hydroxyl group of UDP-N-acetylglucosamine. This pyruvate moiety provides the linker that bridges the glycan and peptide portion ...

*O-Linked β-N-acetylglucosamine

... (O-GlcNAc) is an intracellular carbohydrate that dynamically modifies the amino acids serine and ...

*UDP-N-acetylglucosamine 2-epimerase (hydrolysing)

... (EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase, GNE (gene), siaA (gene), ... UDP-N-acetylglucosamine 2-epimerase (hydrolysing) at the US National Library of Medicine Medical Subject Headings (MeSH) ... Blume, A.; Ghaderi, D.; Liebich, V.; Hinderlich, S.; Donner, P.; Reutter, W.; Lucka, L. (2004). "UDP-N-acetylglucosamine 2- ... Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase". J. Biol. Chem ...

*UDP-3-O-N-acetylglucosamine deacetylase

In molecular biology, UDP-3-O-N-acetylglucosamine deacetylase (also known as UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine ... The structure of UDP-3-O-N-acetylglucosamine deacetylase (LpxC) from Aquifex aeolicus has a two-layer alpha/beta structure ...

*UDP-galactose-UDP-N-acetylglucosamine galactose phosphotransferase

In enzymology, an UDP-galactose-UDP-N-acetylglucosamine galactose phosphotransferase (EC 2.7.8.18) is an enzyme that catalyzes ... "Enzymatic transfer of galactosyl phosphate from UDP-galactose to UDP-N-acetylglucosamine". FEBS Lett. 151 (1): 15-8. doi: ...

*UDP-3-O-acyl-N-acetylglucosamine deacetylase

N-acetylglucosamine deacetylase) is an enzyme with systematic name UDP-3-O-((3R)-3-hydroxymyristoyl)-N-acetylglucosamine ... N-acetylglucosamine deacetylase, UDP-(3-O-acyl)-N-acetylglucosamine deacetylase, UDP-3-O-(R-3-hydroxymyristoyl)-N- ... Jackman, J.E.; Raetz, C.R.; Fierke, C.A. (1999). "UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia ... UDP-3-O-acyl-N-acetylglucosamine deacetylase (EC 3.5.1.108, LpxC protein, LpxC enzyme, LpxC deacetylase, deacetylase LpxC, UDP- ...

*UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase

... (EC 2.7.8.33, UDP-N-acetylglucosamine: ... UDP-N-acetylglucosamine---undecaprenyl-phosphate N-acetylglucosaminephosphotransferase at the US National Library of Medicine ...

*UDP-N-acetylglucosamine-decaprenyl-phosphate N-acetylglucosaminephosphotransferase

UDP-N-acetylglucosamine---decaprenyl-phosphate N-acetylglucosaminephosphotransferase at the US National Library of Medicine ... UDP-N-acetylglucosamine---decaprenyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.35, GlcNAc-1-phosphate ...

*N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase

In enzymology, a N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase (EC 3.1.4.45) is an enzyme that catalyzes ...

*UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase

UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase, and UDP-acetylglucosamine-dolichol phosphate ... Other names in common use include UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate transferase, UDP-GlcNAc:dolichyl- ... Villemez CL, Carlo PL (1980). "Properties of a soluble polyprenyl phosphate UDP-D-N-acetylglucosamine N-acetylglucosamine-1- ... In enzymology, an UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.15) is an enzyme ...
O-linked â-N-acetylglucosamine is a regulatory post translational modification. This modification occurs on nearly all functional classes of proteins, in the nucleus and cytoplasm. O-GlcNAc is added to serine or threonine by O-GlcNAc transferase and removed by O-GlcNAcase. Previous attempts to study O-GlcNAc-modified proteins have resulted in low yields, making 3-dimensional structure determination impossible. In this dissertation O-GlcNAc transferase will be co-expressed with domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2) in E. coli, to produce O-GlcNAc-modified protein. The O-GlcNAc-modified protein was expressed in a variety of E. coli cell lines at a variety of conditions, but only small quantities of insoluble protein were produced. A glycosidase was suspected due to the disappearance of the O-GlcNAc modification from the protein. O-(2-acetamido-2-dexoy-dglucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), a â-N-acetylglucosaminidase
We first attempted to evaluate the overall dynamics of O-GlcNAc on whole protein levels by immunoprecipitation and imunoblotting, but no conclusive result was observed. This may not be surprising because the extent of GlcNAcylation is site-specifically regulated and because O-GlcNAc antibody may not be sensitive enough to recognize significant change of O-GlcNAc on one specific site when the protein is modified on multiple sites. Furthermore, one of the eventual goals of this study is to develop site specific O-GlcNAc antibodies. Thus, we wanted to map O-GlcNAc sites and quantitate O-GlcNAc site specifically. A recently developed chemoenzymatic tagging method was used to enrich O-GlcNAc at peptide levels (17,20). Y289L GalT1 was similarly used to label the GlcNAc moieties as described previously but on trypsin-digested peptides instead of whole proteins. With increased accessibility of the enzyme and donor substrate, the labeling with UDP-GalNAz (an analog of UDP-galactose with azide function ...
NAG Abstracts. Overview » Return to Hemostasis The accompanying papers were presented during a symposium at the Brigham and Womens Hospital, held on 25 February 2003. Taken together the animal and clinical data indicate that poly-N-acetyl glucosamine, an FDA approved agent manufactured by Marine Polymer Technologies Inc. is an effective hemostatic agent whether applied directly to gastric varices; topically against bleeding surfaces of spleen or liver; against major wounds of the abdominal aorta; or somewhat more remotely from the vascular injury, that is on cardiac cathetherization sites in the groin. These studies represent data from animal and human observations. Most of the studies were done in a blinded fashion with proper controls. The only problem with controlling the poly-N-Acetyl glucosamine patch was that it often adhered with somewhat more tenacity than the control cellulose or deacetylated patches. Thus some of the patch effects could be mechanical, although in most studies this ...
Introduction: Aortic valve (AV) disease is a significant contributor to cardiovascular mortality. AV calcification occurs preferentially on the fibrosa side, where endothelial cells (ECs) are subjected to characteristic oscillatory shear stress (OS), whereas the ventricularis ECs experience stable unidirectional laminar shear stress (LS). OS and LS differently regulate endothelial function via gene expression and protein modification. While the post-translational β-N-acetylglucosamine modification of amino acids (O-GlcNAcylation) has been shown to be important in the function of various cell types, its role in AV disease is unknown. We hypothesized that OS impairs EC O-GlcNAcylation, leading to AV inflammation and calcification.. Methods and Results: Immunostaining analysis showed that O-GlcNAcylation was decreased in fibrosa endothelium compared to ventricularis in human and porcine AVs, and human AV ECs (HAVECs) exhibited increased O-GlcNAcylation by LS (20 dyn/cm2) and decreased by OS (+5 ...
The O-GlcNAc (O-linked N-acetylglucosamine) modification is a dynamic and reversible form of protein glycosylation occurring on specific serine and threonine residues of intracellular proteins [1,2]. Since the initial discovery of O-GlcNAc [3], technological advances have greatly facilitated its detection, and proteomics studies [4-6] have shown that a significant proportion of cellular proteins are O-GlcNAcylated. However, the functional importance of O-GlcNAc is only just emerging, with evidence to suggest that it may regulate protein activity in a manner analogous (and complementary) to phosphorylation [7]. O-GlcNAc levels are known to respond dynamically to nutrient availability [1] and stress [8], and to undergo changes during the cell cycle [9] and development [10]. O-GlcNAc has been shown to be associated with a range of human diseases [2]. Strikingly, only two enzymes orchestrate the O-GlcNAc modification. Both the OGT (O-GlcNAc transferase) and its antagonistic OGA (O-GlcNAcase or ...
387537534 - EP 1075836 A3 2001-04-25 - Skin care of food composition containing N-acetyl-glucosamine - [origin: EP1075836A2] The present invention provides a skin care agent comprising N-acetylglucosamine as an active ingredient. The skin care agent is preferably in the form of tablets, capsules, powder such as dust or granules, liquid or paste. The skin care agent of the present invention may be incorporated into foods such as confectioneries, powdered soup and beverages. By orally ingesting the skin care agent of the present invention, the N-acetylglucosamine as an active ingredient is rapidly absorbed, and by utilizing a part thereof as a starting material of acidic mucopolysaccharides such as hyaluronic acid or chondroitin sulfate, the moisture and tension of skin can be improved and the rough skin and fine wrinkles can be prevented or ameliorated.[origin: EP1075836A2] The present invention provides a skin care agent comprising N-acetylglucosamine as an active ingredient. The skin care agent is
Several lectins recognize n-acetyl-glucosamine in a glycoprotein. Based on the linkage and specificity for binding, different N-Acetyl-Glucosamine-binding lectins are utilized to obtain optimum results.
Describes uses for the nutritional supplement N-Acetyl-Glucosamine, side effects it may have, and interactions with foods, medications, or other supplements.
China N-Acetyl-D-Glucosamine, Find details about China N-Acetyl-D-Glucosamine, Glucosamine from N-Acetyl-D-Glucosamine - Yangzhou Rixing Bio-Tech Co., Ltd.
Nutrients regulate gene transcription by the dynamic cycling of O-linked N-acetylglucosamine (O-GlcNAc) on proteins that constitute the transcriptional machinery. A study shows that O-GlcNAcylation of the nuclear factor κB (NF-κB) subunit c-Rel is required for its binding to the promoters of some, but not all, key T cell receptor-dependent genes; however, O-GlcNAcylation is dispensable for the binding of c-Rel to the promoters of tumor necrosis factor-α-dependent genes. This study not only illustrates how specific stimuli that act on the same transcription factor can elicit the expression of particular sets of genes, it also suggests a possible mechanism for autoimmunity in diabetes.. ...
Protein glycosylation is usually relegated to the cell surface and intracellular compartments. In a fascinating exception to this rule that was first observed in the 1980s, A GlcNAc monosaccharide can be added to serine and threonine residues of cytosolic proteins. Many labs are trying to understand the dynamic regulation of the addition and removal of this sugar that seemingly has a hand in every cellular process and disease state known to man. More and more examples are being found to suggest that this modification and phosphorylation regulate each other, as if they werent already complicated enough on their own.. There are a handful of ways to detect O-GlcNAc, which have helped build the laundry list by telling us which proteins are modified. Now, in a recent Nature Chemical Biology paper from Linda Hsieh-Wilsons lab at CalTech, they show us a useful new method that reveals what proportion of any particular protein is modified (2%? 80%), and of those that are modified, exactly how many ...
OGT1_HUMAN] Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the Thr-308 phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating ...
Cancer cells increase nutrient consumption leading to the altered metabolic state known as the Warburg effect. One pathway dependent on glucose, glutamine and acetyl-CoA is the Hexosamine Biosynthetic Pathway (HBP). Increased flux through the HBP leads to elevated post-translation addition of O-linked-β-N-acetylglucosamine (O-GlcNAc) on a diverse population of nuclear and cytosolic proteins, many of which are implicated in cancer. Recently, our lab provided the first evidence that breast and prostate cancers increases total O-GlcNAcylation by increasing O-GlcNAc Transferase (OGT) levels. Importantly, reducing OGT activity inhibits cancer cell invasion in vitro and metastasis in vivo. OGT inhibition reduces breast and prostate cancer cell invasion through, in part, inhibition of the oncogenic transcription factor, FOXM1 and its transcriptional target matrix metalloproteinase 2 (MMP2). Here, we show that OGT regulation of FOXM1 and cancer cell invasion requires regulation of the NAD+-dependent ...
O-GlcNAc transferase antibody [GT2037] (O-linked N-acetylglucosamine (GlcNAc) transferase) for WB. Anti-O-GlcNAc transferase mAb (GTX629813) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
Product Name:N-acetyl-D-(+)-Glucosamine Synonyms:N-Acetyl-Beta-D-Glucosamine; N-Acetyl-D-Glucosamine; 2-Acetamido-2-Deoxy-D-Glucopyranose; N-((1R,2R,3S,4R)-1-Formyl-2,3,4,5-Tetrahydroxy-Pentyl)-Acetamide; N-Acetyl-D-Glucosamine, Immobilized On...
Iex: External Inducer, determined by diffusion through Ficks law (IPTG in our experiment) Iin: Internal Inducer (IPTG) Ii: Inducer bound to Repressor (IPTG bound to lacI) i: Repressor (lacI) Db: Repressor-bound DNA (lacI-bound DNA(CHS3) region in plasmid) Dunb: transcribe-able or Repressor-unbound DNA (lacI-unbound DNA(CHS3)) Re: mRNA for Enzyme (CHS3 mRNA) E: Enzyme (CHS3) S: Substrate (N-Acetyl Glucosamine) C: Enzyme Substrate Complex (CHS3-(N-Acetyl-Glucosamine)-Chitin or (NAG)n Complex) P: Protein Product (Chitin or (NAG)n+1) ...
Many neuronal cytosolic and nuclear proteins are post-translationally modified by the reversible addition of O-linked = 176), demonstrating that cotransfection is a reliable approach in our system. of culturing. Comparison of the staining intensity in neurons expressing dsRED alone (= 23) to that in nontransfected neurons from cultures transfected with either dsRED (= 23) or dsRED + O-GlcNAcase (= 25) did not reveal a difference (> 0.32 and > 0.21 respectively, 2-tailed Welch > 0.25, 2-tailed Welch = 23) to dsRED transfected neurons revealed a 61% decrease in O-GlcNAc staining intensity (< 0.00001, 2-tailed Welch = 140) of O-GlcNAcase over-expressing neurons exhibited one LY310762 supplier or more branches relative to 20% (= 60) of dsRED alone expressing control neurons [Fig. 2(E)]. Thus, decreases in O-GlcNAc levels induced by overexpression of O-GlcNAcase resulted in a 1.85-fold increase in the percentage of neurons that exhibited axon branching. O-GlcNAcase over-expression resulted in a 50% ...
Part of urn:nbn:se:su:diva-968Available from: 2006-04-06 Created: 2006-04-06 Last updated: 2010-01-13Bibliographically approved ...
Hyaluronic acid (HA), a polymer with elastic properties, is a polysaccharide formed from N-acetyl-D-glucosamine and glucuronic acid. HA belongs to a group of chemicals called glycosaminoglycans (GAGs). The activity of a specific form or polymer of HA depends on the size the molecule. HA forms an aggregation center for a large molecule of chondroitin sulfate […]. View Post ...
How protein structure is established is a fascinating question and a field that is actively studied by prominent labs around the world. Protein folding is the process of a chain of amino acids curling into its final shape, and how this process occurs is complex and not completely understood. In general proteins fold depending on their environment (exposed to water or not, for example) and with the help of other proteins, called chaperones. Protein chaperones help to establish a proteins structure as well as maintain it during times of stress. Further, modifications on proteins can change their structures, such as when p53, a protein that is involved in regulating many processes within the cell, is phosphorylated - its structure and, consequently, its function is altered slightly ...
Page contains details about N,N-methylenebisacrylamide-crosslinked poly(N-isopropylacrylamide-co-N-tert-butylacrylamide-co-trisulfated N-acetylglucosamine) hydrogel nanoparticles . It has composition images, properties, Characterization methods, synthesis, applications and reference articles : nano.nature.com
The hexosamine signaling pathway terminating in O-GlcNAc cycling has been implicated in cellular signaling cascades and regulation of transcription and translat...
The long-term objectives of this proposal are to generate and commercialize a new class of high-specificity, high-affinity proteins called Lectenz?, as research...
Sigma-Aldrich offers abstracts and full-text articles by [Caroline Cieniewski-Bernard, Valerie Montel, Serge Berthoin, Bruno Bastide].
The present invention is based on the discovery that hexosamine, and in particular the dynamic O-GlcNAcylation of proteins (modification of proteins by the sugar N-acetylglucosamine) both causes insul
4-O-beta-D-mannopyranosyl-N-acetyl-D-glucosamine + phosphate = N-acetyl-D-glucosamine + alpha-D-mannose 1-phosphate [RN:R10829 ...
Abstract OBJECTIVE: The hexosamine biosynthesis pathway (HBP) flux and protein O-linked N-acetyl-glucosamine (O-GlcNAc) levels have been implicated in mediating the adverse effects..
The cardioprotective capacity and the influence on myocardial O-GlcNAc levels of plasma dialysate from eight healthy volunteers and eight type 2 diabetic patients drawn before and after subjection to an rIPC stimulus were tested on human isolated atrial trabeculae subjected to ischaemia/reperfusion injury. Dialysate from healthy volunteers exposed to rIPC improved post-ischaemic haemodynamic recovery (40 ± 6 vs. 16 ± 2%; P , 0.01) and increased myocardial O-GlcNAc levels. Similar observations were made with dialysate from diabetic patients before exposure to rIPC (43 ± 3 vs. 16 ± 2%; P , 0.001) but no additional cardioprotection or further increase in O-GlcNAc levels was achieved by perfusion with dialysate after exposure to rIPC (44 ± 4 and 42 ± 5 vs. 43 ± 3%; P = 0.7). The glutamine:fructose-6-phosphate amidotransferase (GFAT) inhibitor azaserine abolished the cardioprotective effects and the increment in myocardial O-GlcNAc levels afforded by plasma from diabetic patients and healthy ...
China Antioxidants N-Acetyl-D-Glucosamine for Food Additives, Find details about China N-Acetyl Glucosamine, Arthritis from Antioxidants N-Acetyl-D-Glucosamine for Food Additives - Hefei Reachever Import and Export Limited Company
Cardiosurgery is mostly done under cardiopulmonary bypass. However, the cardiopulmonary bypass and the later recovery of spontaneous circulation, a cardiac ischemia / reperfusion process, may cause myocardial damage and affect cardiac function as well as prognosis.. Glutamine, an amino acid abundant in the human body, plays an important role in the regulation of metabolism and immune cells and the protection of organs. Relative lack of glutamine is reported during stress or serious illness. Animal studies have confirmed that pretreatment with glutamine has a protective effect on the heart, liver, kidney and other organs post ischemia / reperfusion injury. It is also established that glutamine exerts myocardial protection mainly by activating hexosamine biosynthetic pathway, increasing intracellular O-GlcNAc protein modification and expression of heat shock protein 70 (HSP70), starting the protective reaction in the body, improving the function of myocardial cells, and inhibiting the release of ...
N-Acetylglucosaminyltransferase III/MGAT3 products available through Novus Biologicals. Browse our N-Acetylglucosaminyltransferase III/MGAT3 product catalog backed by our Guarantee+.
This gene encodes an enzyme that acts in the lumen of the endoplasmic reticulum to catalyze the transfer of N-acetylglucosamine to serine or threonine residues of extracellular-targeted proteins. This enzyme modifies proteins containing eukaryotic growth factor (EGF)-like domains, including the Notch receptor, thereby regulating developmental signalling. Mutations in this gene have been observed in individuals with Adams-Oliver syndrome 4. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2015 ...
The β-glucoside N,N-diacetylchitobiose is the major breakdown product of chitin, the second most abundant biopolymer after cellulose. E. coli is capable of using N,N-diacetylchitobiose as the sole source of carbon. Chitobiose is imported and concurrently phosphorylated to N,N-diacetylchitobiose 6-phosphate by the chitobiose PTS transporter. Recent evidence suggests that this is followed by deacetylation of the unphosphorylated acetylglucosamine moiety at the reducing end of N,N-diacetylchitobiose 6-phosphate by chito-oligosaccharide mono-deacetylase. N-monoacetylchitobiose 6-phosphate is subsequently hydrolyzed by the glycosyl hydrolase monoacetylchitobiose-6-phosphate hydrolase to D-glucosamine and N-acetyl-D-glucosamine 6-phosphate. N-acetyl-D-glucosamine 6-phosphate enters the N-acetylglucosamine degradation I pathway for conversion to β-D-fructofuranose 6-phosphate, which enters glycolysis. The fate of D-glucosamine is currently unclear; when used as a carbon source, D-glucosamine ...
We have previously reported the substrate specificity of the cytosolic α-D-mannosidase purified from rat liver using Man9GlcNAc, i.e. Manα1-2Manα1-3(Manα1-2Manα1-6)Man α1-6(Manα1-2Manα1-2Manα1-3)Manβ1-4GlcNAc, as substrate [Grard, Saint-Pol, Haeuw, Alonso, Wieruszeski, Strecker and Michalski (1994) Eur. J. Biochem. 223, 99-106]. Man9GlcNAc is hydrolysed giving Man5GlcNAc, i.e. Manα1-2Manα1-2Manα1-3(Manα1-6)Manβ1-4GlcNAc, possessing the same structure as the oligosaccharide of the dolichol pathway formed in the cytosolic compartment during the biosynthesis of N-glycosylprotein glycans. We study here the activity of the purified cytosolic α-D-mannosidase towards the oligosaccharide-diphosphodolichol intermediates formed during the biosynthesis of N-glycans, and also towards soluble oligosaccharides released from the endoplasmic reticulum which are glucosylated or not and possessing at their reducing end either a single N-acetylglucosamine residue or a di-N-acetylchitobiose ...
The protooncogene C-Myc (Myc) regulates cardiac hypertrophy. Myc promotes compensated cardiac function, suggesting that the operative mechanisms differ from those leading to heart failure. Myc regulation of substrate metabolism is a reasonable target, as Myc alters metabolism in other tissues. We hypothesize that Myc-induced shifts in substrate utilization signal and promote compensated hypertrophy. We used cardiac specific Myc-inducible C57/BL6 male mice between 4-6 months old that develop hypertrophy with tamoxifen (tam). Isolated working hearts and 13Carbon (13C )-NMR were used to measure function and fractional contributions (Fc) to the citric acid cycle by using perfusate containing 13C-labeled free fatty acids,more » acetoacetate, lactate, unlabeled glucose and insulin. Studies were performed at pre-hypertrophy (3-days tam, 3dMyc), established hypertrophy (7-days tam, 7dMyc) or vehicle control (cont). Non-transgenic siblings (NTG) received 7-days tam or vehicle to assess drug effect. ...
Hydrolyzes the N-glycolyl group from N-glycolylglucosamine 6-phosphate (GlcNGc-6-P) in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.
Type 2 diabetes mellitus (T2DM) is a well-recognized independent risk factor for heart failure (HF). T2DM is associated with altered cardiac energy metabolism, leading to ectopic lipid accumulation and glucose overload, the exact contribution of these two parameters remaining unclear. To provide new insight into the mechanism driving the development of diabetic cardiomyopathy, we studied a unique model of T2DM: lipodystrophic Bscl2-/- (seipin knockout (SKO)) mice. Echocardiography and cardiac magnetic resonance imaging revealed hypertrophic cardiomyopathy with left ventricular dysfunction in SKO mice and these two abnormalities were strongly correlated with hyperglycemia. Surprisingly, neither intramyocardial lipid accumulation nor lipotoxic hallmarks were detected in SKO mice. 18F-FDG positron emission tomography showed increased myocardial glucose uptake. Consistently, the O-GlcNAcylated protein levels were markedly increased in SKO heart, suggesting a glucose overload. To test this ...
View mouse Pomgnt1 Chr4:116123840-116159849 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
A new technique for detecting proteins modified by β-N-acetyl-D-glucosamine (i.e., O-GlcNAc glycosylation) reveals that the process is reversible and dynamic in neurons and may even play a role in memory. Linda Hsieh-Wilson, California Institute of Technology, Pasadena, and colleagues have developed a quantitative isotopic and chemoenzymatic tagging system (QUIC-Tag) to detect glycosylated proteins inside neurons. Unlike some other methodologies, QUIC-Tag does not require metabolic incorporation of isotopes or rounds of cell division. Cellular levels of O-GlcNAc-proteins are also unperturbed. The technique, which involves protection of the O-GlcNAc moieties by biotinylation followed by avidin-based purification and then mass spectrometry detection, is particularly suited to non-dividing cells, such as neurons.. The technique is explained in detail in the May 13 Nature Chemical Biology online. First author Nelly Khidekel and colleagues also describe how they used the QUIC-Tag method to detect ...
Keratan sulfate (KS) is a glycosaminoglycan (GAG) type consisted of a sulfated poly-N-acetyl lactosamine chain. Besides acting as a constitutive molecule of the extracellular matrices, this GAG also plays a role as a hydrating and signaling agent in
1O9W: The Fimbrial Adhesin F17-G of Enterotoxigenic Escherichia Coli Has an Immunoglobulin-Like Lectin Domain that Binds N-Acetylglucosamine
Wheat germ agglutinin (WGA) is one of the most widely used lectins in cell biology. The receptor sugar for WGA is N-acetylglucosamine, with preferential binding to dimers and trimers of this sugar. WGA can bind oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures which are common to many serum and membrane glycoproteins. Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans, and glycolipids can also bind WGA. Native WGA has also been reported to interact with some glycoproteins via sialic acid residues (see succinylated WGA). ...
In 2014, Gerald Hart, an associate editor for the Journal of Biological Chemistry, organized a thematic minireview series on O-GlcNAcylation. O-GlcNAc is found on many different proteins throughout the cell. Its function varies dependent upon the protein to which it is attached. Much like phosphorylation, one known purpose of O-GlcNAc is to control signaling in response to nutrients. Holt, who is now the chief science officer at NorthShore Bio, describes O-GlcNAc as an orthogonal method of regulating the same proteins: "Its like a rivet: If theres a carbohydrate at a phosphorylation site, then that phosphorylation site is no longer regulated by classical phosphorylation pathways. Instead, it becomes regulated by the O-GlcNAc regulatory pathways.". Methods for studying phosphorylation have advanced rapidly in recent years, thanks in part to the existence of site-specific antibodies, while methods for studying O-GlcNAc continue to lag behind. Researchers only recently have begun to recognize the ...
Pricing for high purity Carbon-13 (13C, C13) and 2H labeled isotopes of N-acetyl-D-glucosamine (GlcNAc) CAS 7512-17-6 from Omicron Biochemicals, Inc.
Mouse Monoclonal Anti-O-GlcNAcase/OGA/MGEA5 Antibody (1C7). Validated: WB, ELISA, ICC/IF. Tested Reactivity: Human. 100% Guaranteed.
GLC 2000 uses high-strength and multiple forms of glucosamine. Find out what advantages this combination of the 4 forms of glucosamine give GLC 2000.
Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins - Volume 70 Issue 1 - A. Pusztai, S. W. B. Ewen, G. Grant, D. S. Brown, J. C. Stewart, W. J. Peumans, E. J. M. Van Damme, S. Bardocz
TY - JOUR. T1 - Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds. AU - Dorfmueller,Helge C.. AU - van Aalten,Daan M. F.. PY - 2010/2/19. Y1 - 2010/2/19. N2 - O-GlcNAcylation is an essential posttranslational modification in metazoa. Modulation of O-GlcNAc levels with small molecule inhibitors of O-GlcNAc hydrolase (OGA) is a useful strategy to probe the role of this modification in a range of cellular processes. Here we report the discovery of novel, low molecular weight and drug-like O-GlcNAcase inhibitor scaffolds by high-throughput screening. Kinetic and X-ray crystallographic analyses of the binding modes with human/bacterial O-GlcNAcases identify some of these as competitive inhibitors. Comparative kinetic experiments with the mechanistically related human lysosomal hexosaminidases reveal that three of the inhibitor scaffolds show selectivity towards human OGA. These scaffolds provide attractive starting points for the development of non-carbohydrate, drug-like OGA ...
Looking for online definition of Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase in the Medical Dictionary? Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase explanation free. What is Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase? Meaning of Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase medical term. What does Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase mean?
Vascular calcification is prevalent in diabetes mellitus and is correlated with adverse cardiovascular outcome32,33; however, the molecular mechanisms underlying increased vascular calcification in diabetes mellitus are largely unknown. Elevation of O-GlcNAcylation is found in human diabetic carotid plaques20 and diabetic mouse vasculature.34 Coincidently, increased vascular calcification has been identified in patients with both type I and type II diabetes mellitus35 and diabetic mouse models.6 Nevertheless, the role of O-GlcNAcylation in vascular calcification has not been previously determined. The present study has demonstrated a causative effect of O-GlcNAcylation on diabetic vascular calcification. Our studies revealed that the activation of AKT by O-GlcNAcylation in vasculature is a key to diabetic vascular calcification. Two novel O-GlcNAcylation sites on AKT play a crucial role in enhancing AKT phosphorylation at S473 to increase vascular calcification. Because O-GlcNAcylation is ...
GlcNAcylation, a post-translational modification in which an O-GlcNAc moiety is added to a serine or threonine residue, is emerging as an important regulator of protein function. Though O-GlcNAc modification is particularly prevalent during conditions of hyperglycemia, as is observed in diabetes, little is known regarding the effects of GlcNAcylation on the function of cardiac signaling proteins. Our lab and others have previously demonstrated that the multifunctional Ca2+/calmodulin dependent protein kinase II (CaMKII), a key regulator of apoptosis and functional remodeling in structural heart disease, is subject to acute, persistent activation by post-translational modification. Here, we test the hypothesis that O-GlcNAc modification modulates CaMKII activity and is upregulated in the failing human heart. We cultured rat cardiomyocytes in either high glucose (4.5g/L) or glucose-free media for 24 hours, followed by lysis and immunoprecipitation using antibodies against CaMKII. Immunoblot of the ...
Looking for online definition of N-acetylglucosamine 6-O-sulfotransferase 4 in the Medical Dictionary? N-acetylglucosamine 6-O-sulfotransferase 4 explanation free. What is N-acetylglucosamine 6-O-sulfotransferase 4? Meaning of N-acetylglucosamine 6-O-sulfotransferase 4 medical term. What does N-acetylglucosamine 6-O-sulfotransferase 4 mean?
Ministry of Human Resource Development (MHRD) under its National Mission on Education through Information and Communication Technology (NMEICT) has initiated the National Digital Library of India (NDL India) pilot project to develop a framework of virtual repository of learning resources with a single-window search facility. Filtered and federated searching is employed to facilitate focused searching so that learners can find out the right resource with least effort and in minimum time. NDL India is designed to hold content of any language and provides interface support for leading Indian languages. It is being arranged to provide support for all academic levels including researchers and life-long learners, all disciplines, all popular form of access devices and differently-abled learners. It is being developed to help students to prepare for entrance and competitive examination, to enable people to learn and prepare from best practices from all over the world and to facilitate researchers to ...
Glucosamine is a naturally occurring amino sugar synthesized in the body from L-glutamine and glucose. Glucosamine stimulates the manufacture of glycosaminoglycans, important components of the cartilage needed for healthy joints. Aging people seem to lose their ability to produce a sufficient amount of glucosamine, and there are no food sources available. Commercial sources of glucosamine are from the exoskeleton of certain shellfish and are available as glucosamine sulfate, glucosamine hydrochloride, and N-acetyl-glucosamine. The sulfated form may most effectively incorporate sulfur into the cartilage. Glycosaminoglycans and glycoproteins allow cells in tissues to hold together. They are necessary for the construction and maintenance of virtually all connective tissues and lubricating fluids in the body. In particular, N-acetyl glucosamine is the final form, which together with glucuronic acid, is polymerized to make the joint lubricant, hyaluronic acid. Chondroitin sulfates provide the
Glucosamine is a naturally occurring amino sugar synthesized in the body from L-glutamine and glucose. Glucosamine stimulates the manufacture of glycosaminoglycans, important components of the cartilage needed for healthy joints. Aging people seem to lose their ability to produce a sufficient amount of glucosamine, and there are no food sources available. Commercial sources of glucosamine are from the exoskeleton of certain shellfish and are available as glucosamine sulfate, glucosamine hydrochloride, and N-acetyl-glucosamine. The sulfated form may most effectively incorporate sulfur into the cartilage. Glycosaminoglycans and glycoproteins allow cells in tissues to hold together. They are necessary for the construction and maintenance of virtually all connective tissues and lubricating fluids in the body. In particular, N-acetyl glucosamine is the final form, which together with glucuronic acid, is polymerized to make the joint lubricant, hyaluronic acid. Chondroitin sulfates provide the
1ZBS: Crystal Structure of the Putative N-acetylglucosamine Kinase (PG1100) from Porphyromonas gingivalis, Northeast Structural Genomics Target PgR18
It is widely accepted that many cancers express features of inflammation, driven by both microenvironmental cells and factors, and the intrinsic production of inflammation-associated mediators from malignant cells themselves. Inflammation results in intracellular oxidative stress, with the ultimate biochemical oxidants composed of reactive nitrogens and oxygens. Although the role of inflammation in carcinogensis is well accepted, we now present data that inflammatory processes are also active in the maintenance phase of many aggressive forms of cancer. The oxidative stress of inflammation is proposed to drive a continuous process of DNA adducts and crosslinks, as well as posttranslational modifications to lipids and proteins that we argue support growth and survival. In this Perspective we introduce data on the emerging science of inflammation-driven posttranslational modifications on proteins responsible for driving growth, angiogenesis, immunosuppression, and inhibition of apoptosis. Examples ...
Analytical high performance liquid affinity chromatography with immobilized neurophysin was used as a molecular screen to evaluate the effects of peptide hormone structure modification on protein recognition. Immobilization of neurophysin on silica and highly cross-linked agarose occurred with retention of oxytocin and vasopressin binding properties. The effects of one-residue-at-a-time mutation, multi-site sequence simplification, and sequence randomization of critical contact residues were evaluated by extent of binding of the peptides on the affinity matrix. The analytical chromatography method also was used as a stereoselective detector to identify racemic contaminants in peptide hormone preparations.. ...
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NAGK Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Also has ManNAc kinase activity. Belongs to the eukaryotic-type N-acetylglucosamine kinase family. Note: This description may include information from UniProtKB ...
This study elaborates upon the finding that C. albicans can utilize N-acetylglucosamine (GlcNAc) to manipulate the environmental pH (29). This phenomenon bears similarities to the extracellular neutralization that results from catabolism of amino acids (28), in the overall magnitude of the pH change, and the excretion of ammonia as a driving force. By genetically blocking the utilization of GlcNAc, either by disrupting the transport from the extracellular environment (ngt1Δ) or by abolishing the enzymes responsible for its catabolism (hxk1Δ, nag1Δ, dac1Δ, or h-d), we have shown that utilization of GlcNAc is required for robust neutralization, as opposed to a strictly signaling role as described for GlcNAc-induced morphogenesis (41). In contrast, none of the described mutations that abolish amino-acid-induced pH changes, including in mutants lacking the Stp2 transcription factor or the Ato1 or Ato5 putative ammonia/acetate transporters (21, 24, 39), affect neutralization in the presence of ...
Shafi, R., Iyer, S. P., Ellies, L. G., ODonnell, N., Marek, K. W., Chui, D., Hart, G. W., and Marth, J. D. (2000). "The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny." Proc Natl Acad Sci U S A. 97, 5735-5739 ...
Learn more about Glucosamine at Regional Medical Center Bayonet Point Supplement Forms/Alternate Names Glucosamine Hydrochloride Glucosamine Sulfate N-Acetyl Glucosamine Uses Principal...
Learn more about Glucosamine at Coliseum Health System Supplement Forms/Alternate Names Glucosamine Hydrochloride Glucosamine Sulfate N-Acetyl Glucosamine Uses Principal...
This formula combines three forms of glucosamine: glucosamine HCl, glucosamine sulfate and n-acetyl-d-glucosamine. These naturally occurring substances build and maintain the matrix of collagen and connective tissue that forms the ground substance of cartilage ...
Chitosanase catalyzes the endohydrolysis of β (1,4) linkages between N-acetyl-D-glucosamine and D-glucosamine residues in partially deacetylated
O‐GlcNAc is a common post‐translational modification of nuclear, mitochondrial, and cytoplasmic proteins that is implicated in the etiology of type II diabetes and Alzheimers disease, as well as cardioprotection
MetabolismCentral intermediary metabolismAmino sugarsglucosamine-6-phosphate deaminase (TIGR00502; EC 3.5.99.6; HMM-score: 33.2) ...
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glucosamine相關商品比價搜尋,Natural Farm自然牧場 紐西蘭頂級天然零食 天然羊肉捲 150g x 2入【藥神網】跑天下錠.含Glucosamine軟骨素,鯊魚軟骨、碳酸鈣和D3於一錠★短效良品-優萃健 寵物營養膏-葡萄糖胺 Glucosamine-120.5g-特價150元 可超取(F673D07)【藥神網】港香蘭 骨天樂膠囊.含Glucosamine葡萄糖胺
glucosamine。相關商品比價搜尋,Natural Farm自然牧場 紐西蘭頂級天然零食 天然羊肉捲 150g x 2入【藥神網】跑天下錠.含Glucosamine軟骨素,鯊魚軟骨、碳酸鈣和D3於一錠【藥神網】港香蘭 骨天樂膠囊.含Glucosamine葡萄糖胺[玉山最低比價網] COSCO KS GLUCOSAMINE PLUS MSM KS 萄萄糖胺 +MSM 240粒 _C637595 $596
Glucosamine is an ingredient recommended for dogs that have problems with arthritis. If a dog no longer enjoys moving around, is lethargic, limps and/or shows signs of pain when touched, then this …. Continue Reading about Whats the Right Glucosamine Dosage for Dogs? → ...
Lots of people take Glucosamine because its a powerful naturally occurring anti-inflammatory. Older dogs often have debilitating aches and pains
I am considering buying some Glucosamine to help with my aging joints. Do any of you take Glucosamine? If so what is the best to take?
Dongguan Bai-tong Hardware Machinery Factory হল সেরা আইভিসি সম্পূরক, Glucosamine সম্পূরক এবং ভিটামিন সি সাপ্লাইমেন্ট সরবরাহকারী, আমরা ভাল মানের পণ্য হয়েছে.
ေဆးပညာအခ်က္အလက္မ်ားကို Hello Sayarwon တြင္ရွာေဖြႏုိင္ျပီး၊ Glucosamine (ဂလူကိုဆာမင္း) , ၏ ေဆးညႊန္းမ်ား၊ ေဘးထြက္ဆိုးက်ိဳးမ်ားႏွင့္သတိေပးခ်က္မ်ားရွာေဖြႏုိင္ပါသည္။
Dinobryon margrave cotter gutturonasal pompster outflank snowy knitted phylacterize Aracana Berteroa Endoceras circuity kinetograph regraduation latinism [email protected] ...
FCN3兔多克隆抗体(ab98136)可与人样本反应并经WB实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
The alteration of glucose metabolism, through increased uptake of glucose and glutamine addiction, is essential to cancer cell growth and invasion. Increased flux of glucose through the Hexosamine Biosynthetic Pathway (HBP) drives increased cellular O-GlcNAcylation (hyper-O-GlcNAcylation) and contributes to cancer progression by regulating key oncogenes. However, the association between hyper-O-GlcNAcylation and activation of these oncogenes remains poorly characterized. Here, we implement a qualitative modeling framework to analyze the role of the Biological Regulatory Network in HBP activation and its potential effects on key oncogenes. Experimental observations are encoded in a temporal language format and model checking is applied to infer the model parameters and qualitative model construction. Using this model, we discover step-wise genetic alterations that promote cancer development and invasion due to an increase in glycolytic flux, and reveal critical trajectories involved in cancer progression
Aspartylglucosaminuria (AGU) is an inherited disease that is characterized by a decline in mental functioning, accompanied by an increase in skin, bone and joint issues. The disease is caused by a defect in an enzyme known as aspartylglucosaminidase. This enzyme plays a significant role in our bodies because it aids in breaking down certain sugars (for example, oligosaccharides) that are attached to specific proteins (for example, glycoproteins). Aspartylglucosaminuria itself is characterized as a lysosomal disease because it does deal with inadequate activity in an enzymes function. Aspartylglucosaminidase functions to break down glycoproteins. These proteins are most abundant in the tissues of the body and in the surfaces of major organs, such as the liver, spleen, thyroid and nerves. When glycoproteins are not broken down, aspartylglucosaminidase backs up in the lysosomes along with other substances. This backup causes progressive damage to the tissues and organs. At birth, there is no sign ...
It is well appreciated that clustering of receptors for the extracellular matrix, most notably the integrins, elicits intracellular signal cascades. One of the first indications that integrin-dependent signaling has occurred is by the activation of focal adhesion kinase (FAK). Another, although less well understood, receptor for the extracellular matrix is (beta)1, 4-galactosyltransferase I (GalT). GalT participates during lamellipodia formation and cell migration by recognizing terminal N-acetylglucosamine residues on basal lamina glycosides. In this study, we investigated whether GalT is also capable of eliciting intracellular signal cascades, specifically FAK activation, in response to ligand binding and/or aggregation. 3T3 fibroblasts were treated with two different reagents capable of aggregating GalT, either antibodies raised against recombinant GalT or multivalent polymers of N-acetylglucosamine, and the effects on tyrosine phosphorylation were analyzed. Both reagents induced an initial ...
E-cadherin is synthesized as a precursor and then undergoes cleavage by proprotein convertases. This processing is essential for E-cadherin maturation and cell adhesion. Loss of cell adhesion causes detachment-induced apoptosis- anoikis. Anoikis can be inhibited despite loss of cell-matrix interactions by preserving E-cadherin mediated cell-cell adhesion. Conversely, acute loss of E-cadherin sensitizes cells to apoptosis by unknown post-translational mechanisms. In response to drug treatment of breast cancer cells, our analysis revealed that two independent modifications of E-cadherin inhibit its cell surface transport. Firstly, O-linked beta-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum. Secondly, incomplete processing by proprotein convertases arrests E-cadherin transport late in the secretory pathway. We demonstrated these E-cadherin modifications (detected by specific lectins and antibodies) do not affect binding to ...
N-Acetyl Glucosamine (NAG) differs from glucosamine sulfate in that it is attached to an acetic acid molecule, while glucosamine sulfate is attached to a sulfuric acid molecule. Although glucosamine sulfate is researched as being better absorbed than NAG, individuals sensitive to sulfur may tolerate NAG better and potentially derive more benefit from its use. NAG is also well recognized for gastrointestinal support by enhancing mucosal integrity.
The biosynthesis of bacterial cell wall peptidoglycan is a complex process involving many different steps taking place in the cytoplasm (synthesis of the nucleotide precursors) and on the inner and outer sides of the cytoplasmic membrane (assembly and polymerization of the disaccharide-peptide monomer unit, respectively). This review summarizes the current knowledge on the membrane steps leading to the formation of the lipid II intermediate, i.e. the substrate of the polymerization reactions. It makes the point on past and recent data that have significantly contributed to the understanding of the biosynthesis of undecaprenyl phosphate, the carrier lipid required for the anchoring of the peptidoglycan hydrophilic units in the membrane, and to the characterization of the MraY and MurG enzymes which catalyze the successive transfers of the N-acetylmuramoyl-peptide and N-acetylglucosamine moieties onto the carrier lipid, respectively. Enzyme inhibitors and antibacterial compounds interfering with ...
The hexosamine biosynthetic pathway, whose end product is UDP-N acetylglucosamine (UDP-GlcNAc), lies at the base of cellular glycosylation pathways, including glycosylation of lipids, formation of heparin sulfated proteoglycans, and N- and O-linked glycosylation of proteins. Forward genetic studies in Drosophila have revealed that mutations in genes encoding different enzymes of the hexosamine biosynthetic pathway result in reduction of UDP-GlcNAc to different extents, with a consequent disruption of distinct glycosylation pathways and developmental processes. A maternal and zygotic loss-of-function screen has identified mutations in nesthocker (nst), which encodes an enzyme in the hexosamine biosynthetic pathway. Embryos lacking maternal and zygotic nst gene products show defective O-GlcNAcylation of a fibroblast growth factor receptor (FGFR)-specific adaptor protein, which impairs FGFR-dependent migration of mesodermal and tracheal cells.. ...
... (MurNAc) is part of the peptidoglycan polymer of bacterial cell walls. MurNAc is covalently linked to N-acetylglucosamine and may also be linked through the hydroxyl on carbon number 4 to the carbon of L-alanine. A pentapeptide composed of L-alanyl-D-isoglutaminyl-L-lysyl-D-alanyl-D-alanine is added to the MurNAc in the process of making the peptidoglycan strands of the cell wall.. Synthesis is inhibited by fosfomycin.[1]. ...
Chitinase Chitinase issue de graines dorge (PDB 1CNS) Les Chitinases (chitodextrinase, 1,4-beta-poly-N-acetylglucosaminidase, poly-beta-glucosaminidase, beta-1,4-poly-N-acetyl glucosamidinase, poly[1,4-(N-acetyl-beta-D-glucosaminide)] glycanohydrolase, (1→4)-2-acetamido-2-deoxy-beta-D-glucan glycanohydrolase) sont des enzymes hydrolitiques qui sattaquent aux liaisons glycosidiques des molécules de chitine. Plus précisément, elles hydrolysent les liaisons (1→4)-β des résidus de N-acétyl-β-D-glucosaminide présents dans la chitine et les chitodextrines. Comme la chitine est le constituant de la paroi cellulaire des mycètes et de lexosquelette de certains animaux comme certains vers et les arthropodes, les chitinases se rencontrent généralement chez les organismes qui ont besoin de remodeler leur propre chitine ou chez ceux qui ont besoin de lyser la chitine dautres organismes. Parmi les organismes qui se nourrissent de chitine, on compte certaines bactéries comme Aeromonas, ...
Shop N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase ELISA Kit, Recombinant Protein and N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc kinase activity.
Glucosamine is a natural compound found in cartilage - the tough tissue that cushions joints.. In supplement form, glucosamine is harvested from shells of shellfish or made in a lab. There are several forms of glucosamine, including glucosamine sulfate, glucosamine hydrochloride and N-acetyl glucosamine. These supplements are not considered interchangeable.. People use glucosamine sulfate orally to treat a painful condition caused by the inflammation, breakdown and eventual loss of cartilage (osteoarthritis).. Research on glucosamine use for specific conditions shows:. ...
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ULTIMATE GLUCOSAMINE is a powder consisting of 100% pure N-acetylglucosamine. This unique formulation contains no additives, salts, preservatives, colouring agents, gluten, lactose or yeast. It dissolves readily and can be added to any hot or cold beverage as a mild sweetener.. N-acetylglucosamine is a major component of hyaluronan, a substance that lubricant joints. It is important in the growth, and repair of joint cartilage and joint damage in experimental models of osteoarthritis1,4.. In addition, it has been shown to have anti-inflammatory properties in vitro. N-acetylglucosamine has been administered to children2 in amounts up to 6 grams per day for up to 2 years without any reported adverse effects.. Lack of adverse effects is likely explained by the fact that N-acetylglucosamine is a natural and important nutritional substance. Human breast milk3 contains as much as 1.5 grams per litre of milk and is the second most abundant sugar after lactose.. ...
Learn more about Glucosamine at Memorial Hospital Supplement Forms/Alternate Names Glucosamine Hydrochloride Glucosamine Sulfate N-Acetyl Glucosamine Uses Principal...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Metabolism drives all biological processes, dysregulation of which fuels a plethora of human diseases including diabetes, obesity, cancer, aging, cardiovascular and neurodegenerative diseases. The long-range goal of our research is to unravel temporal and spatial regulation of metabolic pathways in response to environmental and genetic cues, and to design strategies to battle metabolic diseases. Diet and the light/dark cycle are principle environmental cues that control intermediary metabolism. Nutrient flux into the cell triggers the posttranslational modification of intracellular proteins by the amino sugar called N-acetylglucosamine (O-GlcNAc). Our first goal is to elucidate how O-GlcNAc acts as a molecular switch that couples nutrient cues to cellular regulation of signal transduction, transcription and protein degradation. Both light and diet affect the bodys circadian rhythms. Our second goal is to depict molecular pathways that couple the circadian clock to metabolic physiology. We are ...
Metabolism drives all biological processes, dysregulation of which fuels a plethora of human diseases including diabetes, obesity, cancer, aging, cardiovascular and neurodegenerative diseases. The long-range goal of our research is to unravel temporal and spatial regulation of metabolic pathways in response to environmental and genetic cues, and to design strategies to battle metabolic diseases. Diet and the light/dark cycle are principle environmental cues that control intermediary metabolism. Nutrient flux into the cell triggers the posttranslational modification of intracellular proteins by the amino sugar called N-acetylglucosamine (O-GlcNAc). Our first goal is to elucidate how O-GlcNAc acts as a molecular switch that couples nutrient cues to cellular regulation of signal transduction, transcription and protein degradation. Both light and diet affect the bodys circadian rhythms. Our second goal is to depict molecular pathways that couple the circadian clock to metabolic physiology. We are ...
Chitinases cleave the beta-1-4-glycosidic bond between the N-acetyl-D-glucosamine units of which chitin is comprised. Chitinases are present in plants, bacteria and fungi. The first chitinase structures were solved in 1994, from a bacterium (1ctn) and a plant (2hvm). A mechanism for chitin cleavage was proposed based on several structures and was later confirmed. [1] ...
This study is a withdrawal randomized clinical trail to evaluate the clinical efficacy and safety of 1.1 chemical drugs N-acetyl glucosamine on Chinese IBS-D patients coming from four centers in chongqing. 180 IBS-D patients in this research are accord with the Rome III diagnostic criteria, screening/import period pain intensity scores of the NRS week mean value are 3.0 plus and the days which at least more than one time a stool type are 6 or 7 type over 2 days/week. Test cycle includes screening/import period (2 weeks), open treatment period (8 weeks), a double-blind placebo-controlled randomized withdrawal period (8 weeks), the main outcome measures are pain intensity (NRS score 11 point scale) and stool type ( Bristol type). And secondary endpoints included overall symptoms sensory scores, defecation frequency, abdominal distension, mucous stool and quality of life parameters (IBS-36 scale). After the end of the treatment period, the participants whose pain intensity and stool type are ...
A novel chitin-degrading aerobe, Chitinibacter tainanensis, was isolated from a soil sample from southern Taiwan, and was proved to produce N-acetyl glucosamine (NAG). Chitin degrading factors (CDFs) were proposed to be the critical factors to degrade chitin in this work. When C. tainanensis was incubated with chitin, CDFs were induced and chitin was converted to NAG. CDFs were found to be located on the surface of C. tainanensis. N-Acetylglucosaminidase (NAGase) and endochitinase activities were found in the debris, and the activity of NAGase was much higher than that of endochitinase. The optimum pH of the enzymatic activity was about 7.0, while that of NAG production by the debris was 5.3. These results suggested that some factors in the debris, in addition to NAGase and endochitinase, were crucial for chitin degradation.
Glutamine--fructose-6-phosphate transaminase 1 (GFAT1) catalyzes the formation of glucosamine 6-phosphate. It is the first and rate-limiting enzyme of the hexosamine pathway, in which fructose-6-phosphate is converted to N-acetylglucosamine-6-phosphate. The end-products of the hexosamine pathway are UDP-N-acetylglucosamine (UDP-GlcNAc) and other nucleotide hexosamines. Activation of the hexosamine pathway leads to insulin resistance, largely from deterioration of pancreatic beta-cell function through the induction of oxidative stress. GFAT1 is also known as glutamine:fructose 6 phosphate amidotransferase 1, hexosephosphate aminotransferase 1, D-fructose-6-phosphate amidotransferase 1, GFA, GFAT, GFPT, MSLG, CMSTA1, GFAT1m, and GFPT1L.. ...
The disaccharide Man beta1-4GlcNAc and the trisaccharide Man beta1-4GlcNAc beta1-4GlcNAc were each incubated with CMPNeuAc and rat liver alpha2-6-sialyltransferase (CMP-NeuAc: Gal beta1-4GlcNAc alpha2-6-N-acetylneuraminyl transferase). The resulting mixtures were fractionated by HPLC on Partisil 10 SAX, and the fractions obtained were investigated by TLC, GLC (monosaccharide analysis) and 500-MHz 1H-NMR spectroscopy. ... read more The followingproducts were identified: NeuAc alpha2-6Man beta1-4GlcNAc and NeuAc alpha2-6Man beta1-4GlcNAc beta1-4GlcNAc in yields of 4% and 27%, respectively. The sialylation of Man beta-4GlcNAc-R by Gal beta-4GlcNAc alpha2-6-sialyltransferase contrasts the reported high specificity of this enzyme for the structural element Gal beta1-4GlcNAc of N-linked carbohydrate chains of glycoproteins and related oligosaccharides. show less ...
In the field of biochemistry, O-linked glycosylation is the attachment of a sugar molecule to an oxygen atom in an amino acid residue in a protein. O-linked glycosylation is a form of glycosylation that occurs in the Golgi apparatus in eukaryotes. It also occurs in archaea and bacteria. O-linked glycosylation occurs at a later stage during protein processing, probably in the Golgi apparatus. This is the addition of N-acetyl-galactosamine to serine or threonine residues by the enzyme UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (EC number 2.4.1.41), followed by other carbohydrates (such as galactose and sialic acid). This process is important for certain types of proteins such as proteoglycans, which involves the addition of glycosaminoglycan chains to an initially unglycosylated "proteoglycan core protein." These additions are usually serine O-linked glycoproteins, which seem to have one of two main functions. One function involves secretion to form components of ...
Bacterial peptidoglycans were first identified in the 1940s. The nucleotide precursors were isolated and characterized in 1949. Peptidoglycan biosynthesis has been investigated in many bacterial species. The glycan chains of peptidoglycan are small and repeated units composed of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc). The glmM gene was shown to be essential in Escherichia coli, but genetic data recently suggested that in Staphylococcus aureus there could be an alternative pathway for glucosamine-1-phosphate biosynthesis. The GlmU protein from E. coli is a bifunctional enzyme. Its C-terminal domain catalyzes acetylation of glucosamine-1-phosphate into GlcNAc-1-phosphate, whereas its N-terminal domain catalyzes uridylation to yield UDP-GlcNAc. Nucleoside antibiotics can be subdivided into different classes according to their chemical structures and/or their respective modes of action against MraY: the tunicamycin group, the ribosamino-uridine group, and finally the capuramycin

Uridine Diphosphate N-Acetylglucosamine
     Summary Report | CureHunterUridine Diphosphate N-Acetylglucosamine Summary Report | CureHunter

Uridine Diphosphate N-Acetylglucosamine: Serves as the biological precursor of insect chitin, of muramic acid in bacterial cell ... Acetylglucosamine, UDP; Diphosphate N-Acetylglucosamine, Uridine; Diphospho-N-Acetylglucosamine, Uridine; N-Acetylglucosamine, ... Uridine Diphosphate N-Acetylglucosamine: 13*2,3-dialdehydro-UDP-N-acetylglucosamine. *5-fluoro-2-deoxyuridine diphosphate-N- ... Uridine Diphosphate N-Acetylglucosamine: 13*2,3-dialdehydro-UDP-N-acetylglucosamine. *5-fluoro-2-deoxyuridine diphosphate-N- ...
more infohttp://www.curehunter.com/public/keywordSummaryD014537-Uridine-Diphosphate-N-Acetylglucosamine.do

N-Acetyl Glucosamine - iHerb.comN-Acetyl Glucosamine - iHerb.com

Categories Supplements Amino Acids N-Acetyl Glucosamine N-Acetyl Glucosamine 2 Results (showing 1 - 2 ) ...
more infohttps://www.iherb.com/c/N-Acetyl-Glucosamine

Acetyl Glucosamine | Technology TrendsAcetyl Glucosamine | Technology Trends

Acetyl Glucosamine. Some articles on acetyl, glucosamine:. Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase. ... ... acetyl-glucosamine to the N-acetyl-galactosamine of the Core 1 structure ... are generated by the addition of a single N-acetyl ...
more infohttp://www.primidi.com/acetyl_glucosamine

Side Effects of N-Acetylglucosamine | Livestrong.comSide Effects of N-Acetylglucosamine | Livestrong.com

N-acetylglucosamine supplements are generally considered safe. Minor side effects occur uncommonly and serious side effects are ... N-acetylglucosamine (NAG) is an amino sugar, a derivative of the simple sugar glucose. Your body produces NAG, which serves as ... Side Effects of N-Acetylglucosamine Dr. Tina M. St. John , updated on April 29, 2018 ... N-Acetyl glucosamine is one of the forms of glucosamine. (Image: Farion_O/iStock/GettyImages) ...
more infohttps://www.livestrong.com/article/295135-the-side-effects-of-n-acetyl-glucosamine/

N-Acetyl Glucosamine, 90 capsN-Acetyl Glucosamine, 90 caps

N-Acetyl Glucosamine (NAG) differs from glucosamine sulfate in that it is attached to an acetic acid molecule, while ...
more infohttp://www.herbalremedies.com/n-acetyl-glucosamine.html

UDP-N-acetylglucosamine 2-epimerase domain (IPR003331) | InterPro | EMBL-EBIUDP-N-acetylglucosamine 2-epimerase domain (IPR003331) | InterPro | EMBL-EBI

UDP-N-acetylglucosamine 2-epimerase domain (IPR003331). Short name: UDP_GlcNAc_Epimerase_2_dom ... This entry represents a domain found in the bacterial UDP-N-acetylglucosamine 2-epimerase WecB, which is involved in the ... which has both the UDP-N-acetylglucosamine 2-epimerase and the N-acetylmannosamine kinase functions. GNE catalyses the first ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR003331

Marine Drugs | Free Full-Text | N-Acetylglucosamine: Production and ApplicationsMarine Drugs | Free Full-Text | N-Acetylglucosamine: Production and Applications

N-Acetylglucosamine (GlcNAc) is a monosaccharide that usually polymerizes linearly through (1,4)-β-linkages. GlcNAc is the ... Keywords: N-acetylglucosamine; chitin; carbohydrateN-acetylglucosamine; chitin; carbohydrate N-acetylglucosamine; chitin; ... N-Acetylglucosamine (GlcNAc) is a monosaccharide that usually polymerizes linearly through (1,4)-β-linkages. GlcNAc is the ... Chen, J.-K.; Shen, C.-R.; Liu, C.-L. N-Acetylglucosamine: Production and Applications. Mar. Drugs 2010, 8, 2493-2516. ...
more infohttp://www.mdpi.com/1660-3397/8/9/2493

Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739)Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739)

... to O-Linked N-Acetylglucosamine antibody. Validated in ChIP/Chip, Dot, ICC/IF, IHC-Fr, IP, WB. Clone RL2 referenced in 58 peer- ... Anti-O-Linked N-Acetylglucosamine antibody [RL2] (Alexa Fluor® 488) (ab201993) *Anti-O-Linked N-Acetylglucosamine antibody [RL2 ... Anti-O-Linked N-Acetylglucosamine antibody [RL2]. See all O-Linked N-Acetylglucosamine primary antibodies. ... All lanes : Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739) at 1 µg/ml. Lanes 1 & 3 : Jurkat cells treated with 0 uM ...
more infohttps://www.abcam.com/o-linked-n-acetylglucosamine-antibody-rl2-ab2739.html

acetyl glucosamine | Cosmetic Ingredient Dictionary | Paulas Choiceacetyl glucosamine | Cosmetic Ingredient Dictionary | Paula's Choice

Acetyl glucosamine is a skin-replenishing ingredient that can have considerable value in cosmetic products aimed at diminishing ... Acetyl glucosamine also has research demonstrating that it can have skin-brightening benefits, particularly when combined with ... as their Olay brand uses acetyl glucosamine in select products. Still, the research is compelling and the protocols are sound, ... and both companies sell skincare products that contain acetyl glucosamine. ...
more infohttps://www.paulaschoice.com/ingredient-dictionary/skin-replenishing/acetyl-glucosamine.html

Nutricology, N-Acetyl Glucosamine, 90 Vegetarian Capsules  - iHerb.comNutricology, N-Acetyl Glucosamine, 90 Vegetarian Capsules - iHerb.com

N-Acetyl Glucosamine (NAG). Although research suggests that glucosamine sulfate is better absorbed than NAG, individuals ...
more infohttps://www.iherb.com/pr/Nutricology-N-Acetyl-Glucosamine-90-Vegetarian-Capsules/24558

β-N-acetylglucosamine (O-GlcNAc) is part of the histone code | PNASβ-N-acetylglucosamine (O-GlcNAc) is part of the histone code | PNAS

β-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Kaoru Sakabe, Zihao Wang, and Gerald W. Hart ... O-Linked N-Acetylglucosamine (O-GlcNAc) Transferase and O-GlcNAcase Interact with Mi2{beta} Protein at the A{gamma}-Globin ... O-Linked N-acetylglucosamine transferase 1 regulates global histone H4 acetylation via stabilization of the nonspecific lethal ... O-Linked N-Acetylglucosamine (O-GlcNAc) Expression Levels Epigenetically Regulate Colon Cancer Tumorigenesis by Affecting the ...
more infohttps://www.pnas.org/content/107/46/19915/tab-figures-data

rfbC - UDP-N-acetylglucosamine 2-epimerase - Salmonella borreze - rfbC gene & proteinrfbC - UDP-N-acetylglucosamine 2-epimerase - Salmonella borreze - rfbC gene & protein

UDP-N-acetylglucosamine 2-epimerase (EC:5.1.3.14*Search proteins in UniProtKB for this EC number. ... Belongs to the UDP-N-acetylglucosamine 2-epimerase family.Curated. Family and domain databases. Integrated resource of protein ... sp,P52642,RFBC_SALBO UDP-N-acetylglucosamine 2-epimerase OS=Salmonella borreze OX=55400 GN=rfbC PE=3 SV=1 ...
more infohttps://www.uniprot.org/uniprot/P52642

UDP-N-acetylglucosamine 4-epimerase activity Antibodies | Invitrogen
                       
                       
          ...UDP-N-acetylglucosamine 4-epimerase activity Antibodies | Invitrogen ...

Antibodies for proteins involved in UDP-N-acetylglucosamine 4-epimerase activity pathways, according to their Panther/Gene ... Antibodies for proteins involved in UDP-N-acetylglucosamine 4-epimerase activity pathways; according to their Panther/Gene ...
more infohttps://www.thermofisher.com/antibody/primary/panther/UDP-N-acetylglucosamine%204-epimerase%20activity

RCSB PDB - Protein Feature View 









 - UDP-N-acetylglucosamine 1-carboxyvinyltransferase - B7M095 (MURA ECO8A)RCSB PDB - Protein Feature View - UDP-N-acetylglucosamine 1-carboxyvinyltransferase - B7M095 (MURA ECO8A)

The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
more infohttp://www.rcsb.org/pdb/protein/B7M095

Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase (IPR005882) | InterPro |...Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase (IPR005882) | InterPro |...

N-Acetylglucosamine-1-PO(4) uridyltransferase (GlmU, EC:2.7.7.23) is a trimeric bifunctional enzyme that catalyzes the last two ... Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase (IPR005882). Short name: ... GO:0003977 UDP-N-acetylglucosamine diphosphorylase activity GO:0019134 glucosamine-1-phosphate N-acetyltransferase activity GO: ...
more infohttps://www.ebi.ac.uk/interpro/entry/IPR005882

Alloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase.  - PubMed - NCBIAlloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase. - PubMed - NCBI

Alloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase.. Konrad RJ1, Zhang F, Hale JE, Knierman MD, ... We have previously shown that diabetogenic antibiotic streptozotocin (STZ), an analog of N-acetylglucosamine (GlcNAc), inhibits ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/12054585?dopt=Abstract

N-Acetylglucosamine - WikipediaN-Acetylglucosamine - Wikipedia

N-Acetylglucosamine (N-acetyl-D-glucosamine, or GlcNAc, or NAG) is a monosaccharide and a derivative of glucose. It is an amide ... "Inhibition of elastase enzyme release from human polymorphonuclear leukocytes by N-acetyl-galactosamine and N-acetyl-glucosamine ...
more infohttps://en.wikipedia.org/wiki/N-Acetylglucosamine

GNPTG (N-acetylglucosamine-1-phosphate transferase subunit gamma)GNPTG (N-acetylglucosamine-1-phosphate transferase subunit gamma)

N-acetylglucosamine-1-phosphate transferase subunit gamma), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol ... Golgi membrane UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity Golgi apparatus protein ... Golgi membrane UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity Golgi apparatus protein ...
more infohttp://www.atlasgeneticsoncology.org/Genes/GC_GNPTG.html

GNPTG (N-acetylglucosamine-1-phosphate transferase gamma subunit)GNPTG (N-acetylglucosamine-1-phosphate transferase gamma subunit)

N-acetylglucosamine-1-phosphate transferase gamma subunit), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol ... Golgi membrane UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity Golgi apparatus N-glycan ... Golgi membrane UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity Golgi apparatus N-glycan ...
more infohttp://atlasgeneticsoncology.org/Genes/GC_GNPTG.html

N-Acetyl GlucosamineN-Acetyl Glucosamine

Products tagged with N-Acetyl Glucosamine. Home / Tags / N-Acetyl Glucosamine Popularity. Newest products. Lowest price. ...
more infohttps://www.vitaminexpress.com/tags/n-acetyl-glucosamine/

RCSB PDB 









- 1FXJ: CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE Macromolecule Annotations PageRCSB PDB - 1FXJ: CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE Macromolecule Annotations Page

Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for ... UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE (1FXJ:A,B) * Magnesium Ion Binding * Udp N Acetylglucosamine Diphosphorylase Activity ... UDP N-Acetylglucosamine Acyltransferase; domain 1 Hexapeptide repeat proteins B1. 1fxjB01. Alpha Beta Alpha-Beta Complex Spore ... N-acetylglucosamine 1-phosphate uridyltransferase GlmU, C- terminal domain Escherichia coli [TaxId: 562] ...
more infohttp://www.rcsb.org/pdb/explore/derivedData.do?structureId=1FXJ

N-acetylglucosamine deacetylase - WikipediaN-acetylglucosamine deacetylase - Wikipedia

I. N-Acetylglucosamine deacetylase". J. Biol. Chem. 226: 115-123. PMID 13428742. Molecular and Cellular Biology portal. ... In enzymology, a N-acetylglucosamine deacetylase (EC 3.5.1.33) is an enzyme that catalyzes the chemical reaction N-acetyl-D- ...
more infohttps://en.wikipedia.org/wiki/N-acetylglucosamine_deacetylase

Poly-N-acetylglucosamine mediates biofilm formation and antibiotic resistance in Actinobacillus pleuropneumoniae.  - PubMed -...Poly-N-acetylglucosamine mediates biofilm formation and antibiotic resistance in Actinobacillus pleuropneumoniae. - PubMed -...

Poly-N-acetylglucosamine mediates biofilm formation and antibiotic resistance in Actinobacillus pleuropneumoniae.. Izano EA1, ... Poly-N-acetylglucosamine mediates biofilm formation and antibiotic resistance in Actinobacillus pleuropneumoniae ... Poly-N-acetylglucosamine mediates biofilm formation and antibiotic resistance in Actinobacillus pleuropneumoniae ... Poly-N-acetylglucosamine mediates biofilm formation and antibiotic resistance in Actinobacillus pleuropneumoniae ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/17412552?dopt=Abstract

O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kits | Biocompare.comO-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kits | Biocompare.com

Compare O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kits from leading suppliers on Biocompare. View ... O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a ... Your search returned 3 O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kit across 1 supplier. ...
more infohttps://www.biocompare.com/pfu/110627/soids/2320018/ELISA_Kit/O-linked_N-acetylglucosamine_GlcNAc_transferase_L_homeolog?vcmpv=true

O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kits | Biocompare.comO-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kits | Biocompare.com

Compare O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kits from leading suppliers on Biocompare. View ... O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a ... Your search returned 3 O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kit across 1 supplier. ...
more infohttps://www.biocompare.com/pfu/110627/soids/2320018/ELISA_Kit/O-linked_N-acetylglucosamine_GlcNAc_transferase_L_homeolog?vcmpv=false
  • N -Acetylglucosamine (GlcNAc) is a monosaccharide that usually polymerizes linearly through (1,4)-β-linkages. (mdpi.com)
  • Many cellular proteins, including nuclear pore, oncogene, cytoskeletal, heat shock, viral and transcription regulatory proteins contain single O-linked N-acetylglucosamine (O-GlcNAc) residues attached to serine or threonine residues. (abcam.com)
  • N-Acetylglucosamine (N-acetyl-D-glucosamine, or GlcNAc, or NAG) is a monosaccharide and a derivative of glucose. (wikipedia.org)
  • N-Acetylglucosamine-1-PO(4) uridyltransferase (GlmU, EC:2.7.7.23 ) is a trimeric bifunctional enzyme that catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. (ebi.ac.uk)
  • We have previously shown that diabetogenic antibiotic streptozotocin (STZ), an analog of N-acetylglucosamine (GlcNAc), inhibits the enzyme O-GlcNAc-selective N-acetyl-beta-d-glucosaminidase (O-GlcNAcase) which is responsible for the removal of O-GlcNAc from proteins. (nih.gov)
  • Your search returned 3 O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kit across 1 supplier. (biocompare.com)
  • To develop a drug delivery system targeted to injured blood vessels, we examined whether N -acetylglucosamine (GlcNAc)-bearing polymer-coated liposomes (GlcNAc-Ls) are specifically taken up by vascular smooth muscle cells (VSMCs). (springer.com)
  • Uridine diphosphate-N-acetylglucosamine (uridine 5'-diphosphate-GlcNAc, or UDP-Glc-NAc) is an acetylated aminosugar nucleotide. (hmdb.ca)
  • UDP-GlcNAc is the donor substrate for modification of nucleocytoplasmic proteins at serine and threonine residues with N-acetylglucosamine (O-GlcNAc). (hmdb.ca)
  • Component of the N-acetylglucosamine catabolic cascade that phosphorylates N-acetylglucosamine (GlcNAc), and allows the unique ability to utilise GlcNAc as carbon source. (uniprot.org)
  • It can also be found in the N-terminal region of the mammalian bifunctional protein GNE, which has both the UDP-N-acetylglucosamine 2-epimerase and the N-acetylmannosamine kinase functions. (ebi.ac.uk)
  • N-acetylglucosamine kinase, HXK1 is involved in morphogenetic transition and metabolic gene expression in Candida albicans. (uniprot.org)
  • Kim SJ, Ise H, Goto M, Komura K, Cho CS, Akaike T. Gene delivery system based on highly specific recognition of surface-vimentin with N -acetylglucosamine immobilized polyethylenimine. (springer.com)
  • The effect of N-acetylglucosamine as a substrate for in vitro synthesis of glycosaminoglycans by human peritoneal mesothelial cells and fibroblasts. (supp.ai)
  • Changes in peritoneal mesothelial cells phenotype after chronic exposure to glucose or N-acetylglucosamine. (supp.ai)
  • Here, we report on the targeted imaging and therapy of activated hepatic stellate cells (HSCs) and fibrotic liver tissue using N-acetylglucosamine (GlcNAc)- and indocyanine green (ICG)-conjugated PEI/siRNA complexes. (elsevier.com)