Product Labeling
Skin
Food Labeling
Product Packaging
Spin Labels
Skin Aging
Cosmetics
Substances intended to be applied to the human body for cleansing, beautifying, promoting attractiveness, or altering the appearance without affecting the body's structure or functions. Included in this definition are skin creams, lotions, perfumes, lipsticks, fingernail polishes, eye and facial makeup preparations, permanent waves, hair colors, toothpastes, and deodorants, as well as any material intended for use as a component of a cosmetic product. (U.S. Food & Drug Administration Center for Food Safety & Applied Nutrition Office of Cosmetics Fact Sheet (web page) Feb 1995)
Cosmetic Techniques
Databases, Factual
Extensive collections, reputedly complete, of facts and data garnered from material of a specialized subject area and made available for analysis and application. The collection can be automated by various contemporary methods for retrieval. The concept should be differentiated from DATABASES, BIBLIOGRAPHIC which is restricted to collections of bibliographic references.
N-Acetylglucosaminyltransferases
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.
Glycosylation
Carbohydrate Sequence
Uridine Diphosphate N-Acetylglucosamine
Amino Acid Sequence
Neodymium
Diagnosis, Oral
Biological Products
Chitin
Periodontics
Sulfuric Acids
Datura stramonium
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.
UDPglucose 4-Epimerase
Carbohydrate Epimerases
Salmonella
A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that utilizes citrate as a sole carbon source. It is pathogenic for humans, causing enteric fevers, gastroenteritis, and bacteremia. Food poisoning is the most common clinical manifestation. Organisms within this genus are separated on the basis of antigenic characteristics, sugar fermentation patterns, and bacteriophage susceptibility.
Algorithms
Salmonella typhimurium
Xenopsylla
Transferases (Other Substituted Phosphate Groups)
Rodent Control
Glycomics
Lectins
Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.
Internet
Glycoconjugates
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)
Expression of O-linked N-acetylglucosamine modified proteins and produ by Octavia Y. Goodwin
Dynamic Interplay between O-Linked N-Acetylglucosaminylation and Glycogen Synthase Kinase-3-dependent Phosphorylation |...
Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress: A survival response of mammalian cells -...
GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels<...
Frontiers | FGF23 Induction of O-Linked N-Acetylglucosamine Regulates IL-6 Secretion in Human Bronchial Epithelial Cells |...
Diamond Publications - Search Results
Protein O-GlcNAcylation Is Required for Fibroblast Growth Factor Signaling in Drosophila | Science Signaling
Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α...
Abstract 19733: Shear-Dependent Aortic Valve Endothelial Inflammation and Calcification Are Regulated by O-GlcNAc Modification...
Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc | Science
Human OGA binds substrates in a conserved peptide recognition groove | Biochemical Journal
The lineage stability and suppressive program of regulatory T cells require protein O-GlcNAcylation<...
N-Acetyl-Glucosamine Binding Lectins - GlycoMatrix™
OGT O-linked N-acetylglucosamine (GlcNAc) transferase [Homo sapiens (human)] - Gene - NCBI
Profiling of Protein O-GlcNAcylation in Murine CD8<sup>+</sup> Effector- and Memory-like T...
China N-Acetyl-D-Glucosamine - China N-Acetyl-D-Glucosamine, Glucosamine
Nutrient Regulation of Immunity: O-GlcNAcylation Regulates Stimulus-Specific NF-κB-Dependent Transcription | Science Signaling
Getting a handle on the O-GlcNAc modification - OReilly Science Art, LLC
Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease
3pe4 - Proteopedia, life in 3D
David Vocadlo - Department of Chemistry - Simon Fraser University
Plus it
anti-O-GlcNAc transferase antibody [GT2037] | GeneTex
N-Acetyl-D-Glucosamine (CAS No.: 7512-17-6;134451-94-8); USP - XIAN VEDA CHEMICAL CO.,LTD - ecplaza.net
Team:Northwestern/Project/Modeling - 2010.igem.org
Vegfa | High-Throughput Screen for the Chemical Inhibitors
Deciphering nucleoporin functions in nucleocytoplasmic protein transport in Drosophila.
SAUPAN002586000 - AureoWiki
N-acetyl-D-glucosamine
The Basics of Protein Structure Part 1: The Levels of Structure
O-GlcNAc (CTD110.6) | ALZFORUM
Targeted disruption the enzymes of O-GlcNAc cycling: Animal models of Disease - John Hanover
Development of Research Reagents Specific for O-Glcnac (O-Glcnac Lectenz) - Lori Yang
Kraeber & Co GmbH - N-Acetyl-D-Glucosamine
Early detection of diabetes - The Johns Hopkins University
KEGG ENZYME: 2.4.1.320
Activation of AKT by O-linked N-Acetylglucosamine induces vascular calcification in diabetes mellitus<...
Pomgnt2 (protein O-linked mannose N-acetylglucosaminyltransferase 2 (beta 1,4-)) - Chinchilla Research Resource Database
Impact of O-GlcNAc on cardioprotection by remote ischaemic preconditioning in non-diabetic and diabetic patients. - CARDIO PEG
Inhibition of O-GlcNAc transferase activity reprograms prostate cancer cell metabolism<...
Validity Study of Glutamine to Improve Cardiac Function in Cardiac Surgery - Tabular View - ClinicalTrials.gov
Pomgnt1 (untagged) - Mouse protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase (Pomgnt1), transcript variant 1, ...
Enzymes of N-Acetylglucosamine Metabolism during Germ-tube Formation in Candida albicans | Microbiology Society
Analysis of nucleocytoplasmic protein shuttling by imaging flow cytometry<...
N-Acetylglucosaminyltransferase III/MGAT3 Research Products: Novus Biologicals
EGF domain-specific O-linked N-acetylglucosamine transferase
Oligomannosides or oligosaccharide-lipids as potential substrates for rat liver cytosolic α-d-mannosidase | Biochemical Journal
c-Myc alters substrate utilization and O-GlcNAc protein posttranslational modifications without altering cardiac function...
nagJ - O-GlcNAcase NagJ precursor - Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 /...
Aging | The positive feedback between ACSL4 expression and O-GlcNAcylation contributes to the growth and survival of...
Plus it
Glucosamine
Pomgnt1 MGI Mouse Gene Detail - MGI:1915523 - protein O-linked mannose beta 1,2-N-acetylglucosaminyltransferase
Pomgnt2 MGI Mouse Gene Detail - MGI:2143424 - protein O-linked mannose beta 1,4-N-acetylglucosaminyltransferase 2
Dynamic Glycosylation in Neurons May Be Linked to Memory, Pathology | ALZFORUM
Keratan sulfate: an up-to-date review.
Histone H2B (S112) PAb - GlycoScientific
Lectin
Global (US, EU, Japan & China) N-Acetyl-D-Glucosamine (CAS 7512-17-6) Industry Supply and Consumption 2016 to 2021 Market...
Rapid myoglobin aggregation through... | ERA
Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents...
RCSB PDB - 1W3B: The superhelical TPR domain of O-linked GlcNAc transferase reveals structural similarities to importin alpha.
Journal News: JBC: Probing beneath the surface
O-GlcNAcase/OGA/MGEA5 Antibody (1C7) (H00010724-M02): Novus Biologicals
Study finds low sugar metabolite associates with disability, neurodegeneration in MS
GLC 2000 - ProgressiveHealth.com
Glycoprotein
N-Acetylglucosamine Aminohexose GlcNAc N-Acetylneuraminic acid Aminononulosonic acid. (Sialic acid) NeuNAc ...
N-acetyl-D-glucosamine kinase
N-acetylglucosamine kinase (NAGK; EC 2.7.1.59) converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex ... "Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into ... "N-acetylglucosamine kinase and N-acetylglucosamine 6-phosphate deacetylase in normal human erythrocytes and Plasmodium ... "Entrez Gene: NAGK N-acetylglucosamine kinase". Ligos JM, de Lera TL, Hinderlich S, Guinea B, Sánchez L, Roca R, Valencia A, ...
Glucosamine
"UDP-N-acetylglucosamine Biosynthesis". Recommendations of the Nomenclature Committee of the International Union of Biochemistry ... The end-product of this pathway is uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), which is then used for making ... The intravenous use of a combination of N-acetylglucosamine, pentosan polysulfate and sodium hyaluronate in horses with ... and N-acetylglucosamine. Of the three commonly available forms of glucosamine, only glucosamine sulfate is given a "likely ...
Louise Johnson
Johnson, Louise Napier (1965). An X-ray crystallographic study of N-acetylglucosamine and its relation to lysozyme. london.ac. ... Johnson, L. N.; Phillips, D. C. (1964). "Crystal Structure of N-Acetylglucosamine". Nature. 202 (4932): 588. Bibcode:1964Natur. ... N-Acetylglucosamine, using x-ray diffraction, which she solved within a year. She then moved onto the study of the substrate ...
Glycan
First, two N-acetylglucosamine residues are attached to dolichol monophosphate, a lipid, on the external side of the ... A Core 2 structure is generated by the addition of N-acetyl-glucosamine to the N-acetyl-galactosamine of the Core 1 structure. ... Core 3 structures are generated by the addition of a single N-acetyl-glucosamine to the original N-acetyl-galactosamine. Core 4 ... These are formed by the repetitive addition of galactose and N-acetyl-glucosamine units. Polylactosamine chains on O-linked ...
Oligosaccharyltransferase
The sugar Glc3Man9GlcNAc2 (where Glc=Glucose, Man=Mannose, and GlcNAc=N-acetylglucosamine) is attached to an asparagine (Asn) ...
P110α
Phosphatidylinositol-4,5-bisphosphate 3-kinase (also called phosphatidylinositol 3-kinase (PI3K)) is composed of an 85 kDa regulatory subunit and a 110 kDa catalytic subunit. The protein encoded by this gene represents the catalytic subunit, which uses ATP to phosphorylate phosphatidylinositols (PtdIns), PtdIns4P and PtdIns(4,5)P2.[7] The involvement of p110α in human cancer has been hypothesized since 1995. Support for this hypothesis came from genetic and functional studies, including the discovery of common activating PIK3CA missense mutations in common human tumors.[8] It has been found to be oncogenic and is implicated in cervical cancers.[9] PIK3CA mutations are present in over one-third of breast cancers, with enrichment in the luminal and in human epidermal growth factor receptor 2-positive subtypes (HER2 +). The three hotspot mutation positions (GLU542, GLU545, and HIS1047) have been widely reported till date.[10] While substantial preclinical data show an association with robust ...
Class II PI 3-kinases
... are a subgroup of the enzyme family, phosphoinositide 3-kinase that share a common protein domain structure, substrate specificity and method of activation. Class II PI 3-kinases were the most recently identified class of PI 3-kinases and little is currently known about these enzymes. There are three class II PI 3-kinase isoforms expressed in mammalian cells; ...
Polynucleotide phosphorylase
... (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity.[2] That is, it dismantles the RNA chain starting at the 3' end and working toward the 5' end.[1] It also synthesizes long, highly heteropolymeric tails in vivo. It accounts for all of the observed residual polyadenylation in strains of Escherichia coli missing the normal polyadenylation enzyme.[1] Discovered by Marianne Grunberg-Manago working in Severo Ochoa's lab in 1955, the RNA-polymerization activity of PNPase was initially believed to be responsible for DNA-dependent synthesis of messenger RNA, a notion that got disproved by the late 1950s.[3][4] It is involved in mRNA processing and degradation in bacteria, plants,[5] and in humans.[6] In humans, the enzyme is encoded by the PNPT1 gene. In its active form, the protein forms a ring structure consisting of three PNPase molecules. Each PNPase molecule consists of two ...
Uridine kinase
Thus, the two substrates of this enzyme are ATP and uridine, whereas its two products are ADP and UMP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:uridine 5'-phosphotransferase. Other names in common use include pyrimidine ribonucleoside kinase, uridine-cytidine kinase, uridine kinase (phosphorylating), and uridine phosphokinase. This enzyme participates in pyrimidine metabolism. ...
Galacturonokinase
Thus, the two substrates of this enzyme are ATP and D-galacturonate, whereas its two products are ADP and 1-phospho-alpha-D-galacturonate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-galacturonate 1-phosphotransferase. This enzyme is also called galacturonokinase (phosphorylating) D-galacturonic acid kinase. This enzyme participates in nucleotide sugars metabolism. ...
Glycosaminoglycan
The repeating unit (except for keratan) consists of an amino sugar (N-acetylglucosamine or N-acetylgalactosamine) along with a ...
Taq polymerase
ˈpɒlɪməreɪz/ is a thermostable DNA polymerase named after the thermophilic bacterium Thermus aquaticus from which it was originally isolated by Chien et al. in 1976.[1] Its name is often abbreviated to Taq Pol or simply Taq. It is frequently used in the polymerase chain reaction (PCR), a method for greatly amplifying the quantity of short segments of DNA. T. aquaticus is a bacterium that lives in hot springs and hydrothermal vents, and Taq polymerase was identified[1] as an enzyme able to withstand the protein-denaturing conditions (high temperature) required during PCR.[2] Therefore, it replaced the DNA polymerase from E. coli originally used in PCR.[3] Taq's optimum temperature for activity is 75-80 °C, with a half-life of greater than 2 hours at 92.5 °C, 40 minutes at 95 °C and 9 minutes at 97.5 °C, and can replicate a 1000 base pair strand of DNA in less than 10 seconds at 72 °C.[4] At 75-80 °C, Taq reaches its optimal polymerization rate of about 150 nucleotides per second per ...
Creatine kinase
The mitochondrial creatine kinase (CKm) is present in the mitochondrial intermembrane space, where it regenerates phosphocreatine (PCr) from mitochondrially generated ATP and creatine (Cr) imported from the cytosol. Apart from the two mitochondrial CK isoenzyme forms, that is, ubiquitous mtCK (present in non-muscle tissues) and sarcomeric mtCK (present in sarcomeric muscle), there are three cytosolic CK isoforms present in the cytosol, depending on the tissue. Whereas MM-CK is expressed in sarcomeric muscle, that is, skeletal and cardiac muscle, MB-CK is expressed in cardiac muscle, and BB-CK is expressed in smooth muscle and in most non-muscle tissues. Mitochondrial mtCK and cytosolic CK are connected in a so-called PCr/Cr-shuttle or circuit. PCr generated by mtCK in mitochondria is shuttled to cytosolic CK that is coupled to ATP-dependent processes, e.g. ATPases, such as acto-myosin ATPase and calcium ATPase involved in muscle contraction, and sodium/potassium ATPase involved in sodium ...
Neuraminidase
... inhibitors are useful for combating influenza infection: zanamivir, administered by inhalation; oseltamivir, administered orally; peramivir administered parenterally, that is through intravenous or intramuscular injection; and laninamivir which is in phase III clinical trials. There are two major proteins on the surface of influenza virus particles. One is the lectin haemagglutinin protein with three relatively shallow sialic acid-binding sites and the other is enzyme sialidase with the active site in a pocket. Because of the relative deep active site in which low-molecular-weight inhibitors can make multiple favorable interactions and approachable methods of designing transition-state analogues in the hydrolysis of sialosides, the sialidase becomes more attractive anti-influenza drug target than the haemagglutinin.[9] After the X-ray crystal structures of several influenza virus sialidases were available, the structure-based inhibitor design was applied to discover potent ...
RNA polymerase
... then starts to synthesize the initial DNA-RNA heteroduplex, with ribonucleotides base-paired to the template DNA strand according to Watson-Crick base-pairing interactions. As noted above, RNA polymerase makes contacts with the promoter region. However these stabilizing contacts inhibit the enzyme's ability to access DNA further downstream and thus the synthesis of the full-length product. In order to continue RNA synthesis, RNA polymerase must escape the promoter. It must maintain promoter contacts while unwinding more downstream DNA for synthesis, "scrunching" more downstream DNA into the initiation complex.[14] During the promoter escape transition, RNA polymerase is considered a "stressed intermediate." Thermodynamically the stress accumulates from the DNA-unwinding and DNA-compaction activities. Once the DNA-RNA heteroduplex is long enough (~10 bp), RNA polymerase releases its upstream contacts and effectively achieves the promoter escape transition into the elongation phase. ...
RNA polymerase II holoenzyme
RNAPII can exist in two forms: RNAPII0, with a highly phosphorylated CTD, and RNAPIIA, with a nonphosphorylated CTD.[16] Phosphorylation occurs principally on Ser2 and Ser5 of the repeats, although these positions are not equivalent. The phosphorylation state changes as RNAPII progresses through the transcription cycle: The initiating RNAPII is form IIA, and the elongating enzyme is form II0. While RNAPII0 does consist of RNAPs with hyperphosphorylated CTDs, the pattern of phosphorylation on individual CTDs can vary due to differential phosphorylation of Ser2 versus Ser5 residues and/or to differential phosphorylation of repeats along the length of the CTD.[16] The PCTD (phosphoCTD of an RNAPII0) physically links pre-mRNA processing to transcription by tethering processing factors to elongating RNAPII, e.g., 5′-end capping, 3′-end cleavage, and polyadenylation.[16] Ser5 phosphorylation (Ser5PO4) near the 5′ ends of genes depends principally on the kinase activity of TFIIH (Kin28 in yeast; ...
Serine/threonine-specific protein kinase
While serine/threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific residues to phosphorylate on the basis of residues that flank the phosphoacceptor site, which together comprise the consensus sequence. Since the consensus sequence residues of a target substrate only make contact with several key amino acids within the catalytic cleft of the kinase (usually through hydrophobic forces and ionic bonds), a kinase is usually not specific to a single substrate, but instead can phosphorylate a whole "substrate family" which share common recognition sequences. While the catalytic domain of these kinases is highly conserved, the sequence variation that is observed in the kinome (the subset of genes in the genome that encode kinases) provides for recognition of distinct substrates. Most kinases are inhibited by a pseudosubstrate that binds to the kinase like a real substrate but lacks the amino acid to be phosphorylated. When the pseudosubstrate is ...
UAP1
Mio T, Yabe T, Arisawa M, Yamada-Okabe H (Jul 1998). "The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, ...
Glycoprotein 3-alpha-L-fucosyltransferase
The systematic name of this enzyme class is GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4 ... The difucosylation of asparagine-bound N-acetylglucosamine". Eur. J. Biochem. 199 (3): 745-51. doi:10.1111/j.1432-1033.1991. ... N-acetylglucosamine of, 4-N-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-, acetyl-beta-D-glucosaminyl-(1->2 ... beta-N-acetylglucosamine (Fuc to (Fuc alpha 1--6GlcNAc)-Asn-peptide)alpha 1--3-fucosyltransferase activity in honeybee (Apis ...
Collectin
MBL can recognize peptidoglykan via N-acetylglucosamine. This interaction leads to inhibition of ligand-induced inflammatory by ... "Mannose-binding lectin recognizes peptidoglycan via the N-acetyl glucosamine moiety, and inhibits ligand-induced ...
SGSH
... and N-acetylglucosamine 6-sulfatase (type D; MIM 252940). The Sanfilippo syndrome is characterized by severe central nervous ...
N-Acetylgalactosamine
Galactosamine Globoside (N-Acetylglucosamine) GlcNAc Donald M. Marcus; Elvin A. Kabat; Gerald Schiffman (1964). "Immunochemical ...
N-Acetylmannosamine
By base catalysed epimerization of N-acetyl glucosamine. By rhodium (II)-catalyzed oxidative cyclization of glucal 3-carbamates ... in a commercial process from N-acetylglucosamine. There is normally some level of glycan sialylation within a glycoprotein, but ...
GNPTG
... ("N-acetylglucosamine-1-phosphate transferase, gamma subunit.") is a gene in the human body. It is one of three genes ... also called N-acetylglucosamine-1-phosphate transferase). This enzyme is made up of two alpha (α), two beta (β), and two gamma ...
N-Acetylmuramic acid
MurNAc is a monosaccharide derivative of N-acetylglucosamine. NAM is a combination of N-acetylglucosamine and ... MurNAc is covalently linked to N-acetylglucosamine and may also be linked through the hydroxyl on carbon number 4 to the carbon ... N-Acetylmuramic acid, "NAM" or MurNAc, is the addition of phosphoenolpyruvate and N-acetylglucosamine with the chemical formula ... which is built from alternating units of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc), cross-linked by ...
N-acetylgalactosamine-4-sulfatase
This enzyme also acts on N-acetylglucosamine 4-sulfate. Arylsulfatase B Farooqui AA (October 1976). "The desulphation of ...
UDP-glucose 4-epimerase
Accommodation of UDP-N-acetylglucosamine within the active site". J. Biol. Chem. 276 (18): 15131-6. doi:10.1074/jbc.M100220200 ... from UDP-N-acetylglucosamine (UDP-GlcNAc) in the presence of NAD+, an initial step in glycoprotein or glycolipid synthesis. Dr ...
Paenibacillus tylopili
It lacks the ability to break down N-acetylglucosamine. Kuisiene N, Raugalas J, Spröer C, Kroppenstedt RM, Stuknyte M, ...
Poly(ribitol-phosphate) N-acetylglucosaminyl-transferase
Other names in common use include UDP acetylglucosamine-poly(ribitol phosphate), acetylglucosaminyltransferase, uridine ... Nathenson SG, Ishimoto N, Strominger JL (1966). "UDP-N-acetylglucosamine:polyribitol phosphate N-acetylglucosaminyltransferases ...
N-Acetylglucosamine - Wikipedia
N-Acetylglucosamine (GlcNAc) is an amide derivative of the monosaccharide glucose. It is a secondary amide between glucosamine ... O-GlcNAcylation is the process of adding a single N-acetylglucosamine sugar to the serine or threonine of a protein.[4] ... Comparable to phosphorylation, addition or removal of N-acetylglucosamine is a means of activating or deactivating enzymes or ... "Inhibition of elastase enzyme release from human polymorphonuclear leukocytes by N-acetyl-galactosamine and N-acetyl-glucosamine ...
EWG Skin Deep® | What is ACETYL GLUCOSAMINE
N-Acetylglucosamine receptor - Wikipedia
The N-Acetylglucosamine receptor is a receptor which binds N-Acetylglucosamine. The N-Acetylglucosamine (GlcNAc) receptor has ... N-Acetylglucosamine+Receptor at the US National Library of Medicine Medical Subject Headings (MeSH) v t e. ... "Targeted gene delivery via N-acetylglucosamine receptor mediated endocytosis". Journal of Nanoscience and Nanotechnology. 14 ( ...
N-Acetyl Glucosamine - iHerb.com
Products That Contain ACETYL GLUCOSAMINE || Skin Deep® Cosmetics Database | EWG
UDP-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 ...
N-Acetyl Glucosamine (Nag): Uses, Side Effects, Interactions, Dosage, and Warning
Medications for cancer (Chemotherapy) interacts with N-ACETYL GLUCOSAMINE (NAG). There is some concern that N-acetyl ... Chitosan is a form of N-acetyl glucosamine that has been chemically altered.. N-acetyl glucosamine is used for osteoarthritis, ... N-ACETYL GLUCOSAMINE (NAG). OTHER NAME(S): 2-Acetamido-2-deoxyglucose, Acetylglucosamine, Acétylglucosamine, GlcNAc, ... When applied to the skin: N-acetyl glucosamine is POSSIBLY SAFE when used for up to 10 weeks.. When given as an enema (rectally ...
Topical composition comprising n-acetyl glucosamine - YU RUEY J
4. Effect of N-acetyl-glucosamine on skin. A female subject, age 74, applied topically twice daily 10% N-acetyl-glucosamine ... The white cream thus formulated contained 10% N-acetyl-glucosamine. N-Acetyl-glucosamine 1% or 5% cream was formulated in the ... A male subject, age 66, who had xerosis and dry skin on lower legs topically applied twice daily 5% N-acetyl-glucosamine cream ... 7. A water-containing composition comprising N-acetyl-glucosamine as isomeric or non-isomeric form thereof and a vitamin in a ...
Side 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) ...
β-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 ...
OGT O-linked N-acetylglucosamine (GlcNAc) transferase [Homo sapiens (human)] - Gene - NCBI
O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase). O- ... UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase. uridinediphospho-N-acetylglucosamine:polypeptide beta-N- ... OGT O-linked N-acetylglucosamine (GlcNAc) transferase [Homo sapiens] OGT O-linked N-acetylglucosamine (GlcNAc) transferase [ ... O-linked N-acetylglucosamine (GlcNAc) transferaseprovided by HGNC. Primary source. HGNC:HGNC:8127 See related. Ensembl: ...
Marine 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. ...
RCSB PDB - 2JF2: Nucleotide substrate binding by UDP-N-acetylglucosamine acyltransferase
ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE. A. 264. Escherichia coli. Mutation(s): 0 EC: 2.3.1.129 ... UDP-N-acetylglucosamine acyltransferase (LpxA) initiates lipid A biosynthesis by catalyzing the transfer of R-3-hydroxymyristic ... UDP-N-acetylglucosamine acyltransferase (LpxA) initiates lipid A biosynthesis by catalyzing the transfer of R-3-hydroxymyristic ... Nucleotide Substrate Recognition by Udp-N-Acetylglucosamine Acyltransferase (Lpxa) in the First Step of Lipid a Biosynthesis.. ...
Acetyl Glucosamine | Technology Trends
Nutricology, N-Acetyl Glucosamine, 90 Vegetarian Capsules - iHerb.com
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: ...
Alloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase. - PubMed - NCBI
N-Acetyl Glucosamine, 90 caps
N-acetylglucosamine-1-phosphotransferase, gamma subunit Biomolecules | Biocompare
Compare N-acetylglucosamine-1-phosphotransferase, gamma subunit Biomolecules from leading suppliers on Biocompare. View ... N-Acetylglucosamine-1-Phosphate Transferase, gamma Subunit (GNPTG) (AA 25-307) protein (His tag) ... Your search returned 5 N-acetylglucosamine-1-phosphotransferase, gamma subunit Biomolecules across 4 suppliers. ...
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 ...
rfbC - 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 ...
RCSB 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] ...
Regulation of N-acetylglucosamine Uptake in Yeast
The yeasts unable to grow on N-acetylglucosamine lacked the capacity to transport the aminosugar … ... Various yeasts have been investigated for their ability to grow on N-acetylglucosamine as the sole carbon source and only those ... Regulation of N-acetylglucosamine Uptake in Yeast Biochim Biophys Acta. 1979 Oct 19;557(1):248-58. doi: 10.1016/0005-2736(79) ... Various yeasts have been investigated for their ability to grow on N-acetylglucosamine as the sole carbon source and only those ...
acetyl glucosamine | Cosmetic Ingredient Dictionary | Paula's Choice
Although pure acetyl glucosamine is considered unstable, a synthetic or bio-fermented derivative known as n-acetyl glucosamine ... Acetyl glucosamine is an amino-monosaccharide (simple sugar) and a precursor of hyaluronic acid (meaning it helps skin make ... Acetyl glucosamine has also been shown to be effective in reducing visible discolorations when paired with the B vitamin ... pure acetyl glucosamine is typically derived from shellfish). ...
Amdhd2 - N-acetylglucosamine-6-phosphate deacetylase - Rattus norvegicus (Rat) - Amdhd2 gene & protein
N-acetylglucosamine-6-phosphate deacetylaseAdd BLAST. 409. Proteomic databases. jPOST - Japan Proteome Standard Repository/ ... N-acetylglucosamine catabolic process Source: GO_Central ,p>Inferred from Biological aspect of Ancestor,/p> ,p>A type of ... N-acetylglucosamine-6-phosphate deacetylaseBy similarity. Manual assertion inferred from sequence similarity toi ... sp,Q5BJY6,NAGA_RAT N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2 ...
N-Acetylglucosamine - Lectins - Lectins & Glycobiology Reagents - All Products
Targeting N-acetylglucosamine-bearing polymer-coated liposomes to vascular smooth muscle cells | SpringerLink
Drug delivery system N-acetylglucosamine Lectin Restenosis Vascular smooth muscle cells This is a preview of subscription ... Kobayashi S, Ise H, Takahashi M, Goto M, Akaike T, Ikeda U. Surface coating of bone marrow cells with N-acetylglucosamine for ... Aso S, Ise H, Takahashi M, Kobayashi S, Morimoto H, Izawa A, Goto M, Ikeda U. Effective uptake of N-acetylglucosamine- ... To develop a drug delivery system targeted to injured blood vessels, we examined whether N-acetylglucosamine (GlcNAc)-bearing ...
Source Naturals N-A-G, N-Acetyl Glucosamine at Netrition.com.
GlcNAcProteinsSubunitUridine diphosphate N-acetylglucosamineResiduesEnzymeKinaseBeta-N-acetylglucosaminePeptidoglycanPyrophosphorylaseThreonineAntibodyGeneProteinPhosphorylationBindsBacterialBiosynthetic pathwayPathwaysEnolpyruvylUptakeReceptorDerivativePhosphate groupsEscherichiaMonosaccharideGlucoseSequenceActivityProductionForm
GlcNAc33
- N -Acetylglucosamine (GlcNAc) is an amide derivative of the monosaccharide glucose . (wikipedia.org)
- The N-Acetylglucosamine (GlcNAc) receptor has been recently found to interact and bind with vimentins at the cell surface. (wikipedia.org)
- Uridine diphosphate release mechanism in O-N-acetylglucosamine (O-GlcNAc) transferase catalysis. (nih.gov)
- N -Acetylglucosamine (GlcNAc) is a monosaccharide that usually polymerizes linearly through (1,4)-β-linkages. (mdpi.com)
- 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)
- 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)
- 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)
- Your search returned 3 O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kit across 1 supplier. (biocompare.com)
- N -acetylglucosamine (GlcNAc), the vital signaling molecule controlling the onset of development and antibiotic synthesis in Streptomyces , was found to increase the yields of bleomycins significantly in chemically defined medium. (springer.com)
- O -Linked N -acetylglucosaminylation ( O -GlcNAcylation) (or O -linked N -acetylglucosamine ( O -GlcNAc)) is an abundant and reversible glycosylation type found within the cytosolic and the nuclear compartments. (mcponline.org)
- The hexosamine biosynthetic pathway (HBP) generates the substrate for the O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins. (frontiersin.org)
- Once activated, the HBP generates the sugar nucleotide UDP-N-acetyl-glucosamine (UDP-GlcNAc), which is a substrate for hyaluronan (HA), N-linked glycosylation, and for the O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins ( 17 ). (frontiersin.org)
- 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)
- The aim of the present study was to evaluate the anti‑inflammatory effects of citrulline (Cit), glucosamine (GlcN) and N‑acetylglucosamine (GlcNAc) on synovial cells, which are primarily involved in inflammatory joint diseases. (spandidos-publications.com)
- N-acetylglucosamine (GlcNAc), a derivative of GlcN, exhibits anti-inflammatory and chondroprotective effects in a rat model of OA by reducing IL-6 production, cyclooxygenase expression and type II collagen degradation ( 12-15 ). (spandidos-publications.com)
- Immunoblot analysis using an antibody generated against human IRS-1 Ser 1011 GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as β- N -acetylglucosamine. (mcponline.org)
- Our study investigated the effect of N-acetylglucosamine (GlcNAc) on the intestinal mucosal barrier function in rats. (banglajol.info)
- O-linked N -acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins. (portlandpress.com)
- Uridine diphosphate N-acetylglucosamine (GlcNAc) is the product of the hexosamine biosynthetic pathway and the substrate for O-linked GlcNAc (O-GlcNAc) modification. (molvis.org)
- As an initial step to identify plant NPC proteins, we examined whether NPC proteins from tobacco are modified by N-acetylglucosamine (GlcNAc). (plantcell.org)
- Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code. (semanticscholar.org)
- Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions. (semanticscholar.org)
- In studies on mice, Dr. Michael Demetriou and colleagues with the UC Irvine Center for Immunology found that N-acetylglucosamine (GlcNAc), which is similar but more effective than the widely available glucosamine, inhibited the growth and function of abnormal T-cells that incorrectly direct the immune system to attack specific tissues in the body, such as brain myelin in MS and insulin-producing cells of the pancreas in diabetes. (thisisms.com)
- To study the effect of short N -acetylglucosamine (GlcNAc) oligosaccharides on the physiology of plants, N-ACETYLGLUCOSAMINYLTRANSFERASE ( NodC ) of Azorhizobium caulinodans was expressed in Arabidopsis ( Arabidopsis thaliana ). (plantphysiol.org)
- Catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. (mybiosource.com)
- Also known as N-acetylmuramic acid/N-acetylglucosamine kinase (MurNAc/GlcNAc kinase) (Murein sugar kinase). (mybiosource.com)
- Antiporter transporting nucleotide sugars such as UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-glucose (UDP-Glc) and GDP-mannose (GDP-Man) pooled in the cytosol into the lumen of the Golgi in exchange for the corresponding nucleosides monophosphates (UMP for UDP-sugars and GMP for GDP-sugars). (mybiosource.com)
- Structures of Bacteroides fragilis uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA). (escholarship.org)
- Uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes a reversible reaction for adding an O-acyl group to the GlcNAc in UDP-GlcNAc in the first step of lipid A biosynthesis. (escholarship.org)
- O-linked N-acetylglucosamine transferase (OGT), an enzyme used for addition of O-GlcNAc during O-GlcNAcylation, is identified as a key regulator to promote oncogenesis in a feedback mechanism through the stabilization of c-Myc. (peerj.com)
- Objective: There is increasing evidence that the addition of O-linked N-acetylglucosamine (O-GlcNAc) to proteins plays an important role in cell signaling pathways. (elsevier.com)
Proteins5
- In Western blot many bands are expected as the O-Linked N-Acetylglucosamine modification can occur on proteins of different sizes. (abcam.com)
- Hart GW, Housley MP, Slawson C. Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. (banglajol.info)
- Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine. (plantcell.org)
- Hyperglycemia, a hallmark of diabetes mellitus, is associated with increased vascular calcification and increased modification of proteins by O-linked N-acetylglucosamine (O-GlcNAcylation). (ahajournals.org)
- O-Linked beta-N-acetylglucosamine transferase (OGT) levels are highest in the brain, and neurodegenerative disorders such as Alzheimer disease have been shown to involve abnormally phosphorylated key proteins, probably as a result of hypoglycosylation. (antibody-antibodies.com)
Subunit5
- Your search returned 5 N-acetylglucosamine-1-phosphotransferase, gamma subunit Biomolecules across 4 suppliers. (biocompare.com)
- 9 We have previously ascribed ML III type C to mutations in the UDP -N- acetylglucosamine-1-phosphotransferase gamma subunit gene (GNPTAG) on chromosome 16p. (bmj.com)
- We suggest that, although the exact relative frequency of each ML III type is not known, the UDP -N- acetylglucosamine-1-phosphotransferase gamma subunit gene apparently plays a major role in mucolipidosis type III. (bmj.com)
- A gene on chromosome 12q23.2 that encodes two of three subunit types of the membrane-bound enzyme N-acetylglucosamine-1-phosphotransferase, a heterohexameric complex composed of 2 alpha, 2 beta and 2 gamma subunits. (thefreedictionary.com)
- This is mostly due to the stabilyty of the standard of the Rat UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit(OGT) ELISA kit. (antibody-antibodies.com)
Uridine diphosphate N-acetylglucosamine1
- Toxin ζ expression triggers a reversible state of dormancy, diminishes the pool of purine nucleotides, promotes (p)ppGpp synthesis, phosphorylates a fraction of the peptidoglycan precursor uridine diphosphate-N-acetylglucosamine (UNAG), leading to unreactive UNAG-P, induces persistence in a reduced subpopulation, and sensitizes cells to different antibiotics. (mdpi.com)
Residues3
- This gene encodes a glycosyltransferase that catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. (nih.gov)
- When developing cotyledons are labeled with [3H]glucosamine and glycopeptides of PHA present in the Golgi complex isolated, the radioactivity can be released as [3H]N-acetylglucosamine by digestion of the glycopeptides with beta-N-acetylglucosaminidase, indicating that the residues are in a terminal position. (rupress.org)
- Arrival of PHA in the protein bodies is followed by the slow removal of these terminal N-acetylglucosamine residues, resulting in a decrease in the Mr of the modified sidechains. (rupress.org)
Enzyme6
- Alloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase. (nih.gov)
- Here we present that stable knock-down of UDP- N -acetylglucosamine 2-epimerase / N -acetylmannosamine kinase ( GNE ), the key enzyme in the sialic acid biosynthetic pathway, dramatically increases incorporation of N -acetylmannosamine analogues into glycoproteins of HEK293 cells . (rsc.org)
- Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ. (harvard.edu)
- 3, 4 The UDP -N- acetylglucosamine-1-phosphotransferase enzyme activity is defective in ML III 6 and three complementation groups (A, B, C) have been reported suggesting genetic heterogeneity. (bmj.com)
- 6, 8 In 1996, Bao et al 9 showed that UDP -N- acetylglucosamine-1-phosphotransferase is a multimeric enzyme made up of three different subunits. (bmj.com)
- Further, it was demonstrated that the activity of the precursor-producing enzyme UDP-N-acetylglucosamine 4-epimerase, converting UDP-N-acetylglucosamine into UDP-N-acetylgalactosamine, is responsible for the presence of N-acetylgalactosamine in the EPS repeating units of both strains. (hud.ac.uk)
Kinase4
- 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)
- Similar results were obtained with Saccharomyces cerevisiae 3059 and some other yeasts which are devoid of N-acetylglucosamine kinase in both uninduced and induced conditions. (nih.gov)
- Below are the list of possible N-acetylmuramic acid/N-acetylglucosamine kinase products. (mybiosource.com)
- N-acetylglucosamine kinase [Source:HGNC Sym. (broadinstitute.org)
Beta-N-acetylglucosamine2
- GENTAUR antibody-antibodies.com The Marketplace for Antibodies : Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain. (antibody-antibodies.com)
- Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain. (antibody-antibodies.com)
Peptidoglycan2
- Six of these homologues have been proposed to be peptidoglycan N-acetylglucosamine deacetylases. (pasteur.fr)
- This is the first biochemical study of bacterial peptidoglycan N-acetylglucosamine deacetylases. (pasteur.fr)
Pyrophosphorylase3
- A search of the yeast data base for a protein homologous to Escherichia coli UDP-N-acetylglucosamine pyrophosphorylase yielded UAP1 (UDP-N-acetylglucosamine pyrophosphorylase), the Saccharomyces cerevisiae gene for UDP-N-acetylglucosamine pyrophosphorylase. (semanticscholar.org)
- Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily. (semanticscholar.org)
- UDP-N-acetylglucosamine pyrophosphorylase 1. (broadinstitute.org)
Threonine1
- O-GlcNAcylation is the process of adding a single N -acetylglucosamine sugar to the serine or threonine of a protein. (wikipedia.org)
Antibody1
- N-Acetylglucosamine antibody LS-C505218 is an AP-conjugated mouse monoclonal antibody to human N-Acetylglucosamine. (lsbio.com)
Gene1
- 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)
Protein3
- Also known as UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter (Homolog of Fringe connection protein 1) (HFRC1) (SQV7-like protein) (SQV7L) (Solute carrier family 35 member D2) (UDP-galactose transporter-related protein 8) (UGTrel8). (mybiosource.com)
- UDP-acetylglucosamine acts as a donor for the first two steps of the N-glycan precursor biosynthesis pathway, and is later used as a substrate for further modifications after the precursor has been attached to the protein. (reactome.org)
- Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: attachment in the Golgi apparatus and removal in protein bodies. (rupress.org)
Phosphorylation1
- [4] Comparable to phosphorylation , addition or removal of N -acetylglucosamine is a means of activating or deactivating enzymes or transcription factors . (wikipedia.org)
Binds2
- The N-Acetylglucosamine receptor is a receptor which binds N-Acetylglucosamine. (wikipedia.org)
- Uranyl acetate (0.01 mM) which binds to cell membrane-associated polyphosphates, inhibited completely the inducible uptake of N-acetylglucosamine. (nih.gov)
Bacterial1
- This entry represents a domain found in the bacterial UDP-N-acetylglucosamine 2-epimerase WecB, which is involved in the enterobacterial common antigen biosynthesis [ PMID: 2166030 ]. (ebi.ac.uk)
Biosynthetic pathway1
- Nutrient sensing in mammals is done through the hexosamine biosynthetic pathway (HSP), which produces uridine 5'-diphospho-N-acetylglucosamine (UDP-Glc-NAc) as its end product. (hmdb.ca)
Pathways1
- The chemical reactions and pathways involving N-acetylglucosamine. (broadinstitute.org)
Enolpyruvyl1
- Adds enolpyruvyl to UDP-N-acetylglucosamine. (rcsb.org)
Uptake3
- In pathogenic yeasts, two systems of different affinity for substrate were found to operate in the uptake of N-acetylglucosamine. (nih.gov)
- In glucose-grown Candida albicans cells which are devoid of N-acetylglucosamine enters into the cells as phosphorylated form using a constitutive uptake system. (nih.gov)
- Furthermore, inhibitors of energy metabolism (arsenate, azide and cyanide), proton conductor (m-chlorocarbonylcyanide phenylhydrazine) and dibenzyl diammonium ion (membrane permeable cation) inhibited the inducible N-acetylglucosamine uptake in C. albicans. (nih.gov)
Receptor2
- Return to N-Acetylglucosamine receptor . (wikidoc.org)
- Thus, ASA receives N -acetylglucosamine 1-phosphate groups in a sequential manner at two or more sites located within the secretory route proximal and distal to the site where ASA is retrieved by the KDEL receptor, i.e. proximal to the trans -Golgi. (biochemj.org)
Derivative1
- N-acetylglucosamine (NAG) is an amino sugar, a derivative of the simple sugar glucose. (livestrong.com)
Phosphate groups2
- At each of these sites up to two N -acetylglucosamine 1-phosphate groups can be added to a single oligosaccharide. (biochemj.org)
- The biosynthetic intermediates of the glycoproteins destined for the lysosomal compartments of animal cells contain high-mannose sidechains modified by phosphate groups covered by N-acetylglucosamine that is labile to mild acid treatment. (rupress.org)
Escherichia1
- A Poly-N-acetylglucosamine-Shiga toxin broad-spectrum conjugate vaccine for Shiga toxin-producing Escherichia coli. (surrey.ac.uk)
Monosaccharide1
- Structural studies including monosaccharide and phosphate analysis, glycosidase and phosphatase treatments, methylation analysis, and periodate treatment indicated the structure of this compound to be NeuAc alpha 2-6Gal beta 1-4GlcNAc-6-P. This provides the first evidence for the occurrence of N-acetylglucosamine 6-phosphate as an integral component in complex carbohydrates. (nih.gov)
Glucose2
- Ciszewicz M, Wu G, Tam P, Polubinska A, Breborowicz A. Changes in peritoneal mesothelial cells phenotype after chronic exposure to glucose or N-acetylglucosamine. (banglajol.info)
- Below are the list of possible UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter products. (mybiosource.com)
Sequence1
- Labelling experiments, designed to determine the temporal sequence of appearance of N-acetylglucosamine in intracellular free sugar and sugar-phosphate pools, indicated that N-acetylglucosamine first appeared in the cells as pohosphorylated form. (nih.gov)
Activity1
- The activity of UDP-N-acetylglucosamine 4-epimerase was higher in both S. thermophilus strains than in a non-EPS-producing control strain. (hud.ac.uk)
Production2
Form1
- Today I just got two jars of Ultimate Glubosamine (n-acetylglucosamine form) in the mail. (thisisms.com)