Acetylglucosaminidase: A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.Genomic Structural Variation: Contiguous large-scale (1000-400,000 basepairs) differences in the genomic DNA between individuals, due to SEQUENCE DELETION; SEQUENCE INSERTION; or SEQUENCE INVERSION.Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.Glycoconjugates: Carbohydrates covalently linked to a nonsugar moiety (lipids or proteins). The major glycoconjugates are glycoproteins, glycopeptides, peptidoglycans, glycolipids, and lipopolysaccharides. (From Biochemical Nomenclature and Related Documents, 2d ed; From Principles of Biochemistry, 2d ed)Hexosaminidases: Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.Endo-1,4-beta Xylanases: Enzymes which catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in XYLANS.N-Acetylmuramoyl-L-alanine Amidase: An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.Glycoside HydrolasesPeptidoglycanAcetylglucosamine: The N-acetyl derivative of glucosamine.Mucopolysaccharidosis III: Mucopolysaccharidosis characterized by heparitin sulfate in the urine, progressive mental retardation, mild dwarfism, and other skeletal disorders. There are four clinically indistinguishable but biochemically distinct forms, each due to a deficiency of a different enzyme.Mucopolysaccharidoses: Group of lysosomal storage diseases each caused by an inherited deficiency of an enzyme involved in the degradation of glycosaminoglycans (mucopolysaccharides). The diseases are progressive and often display a wide spectrum of clinical severity within one enzyme deficiency.Phosphoric Diester Hydrolases: A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. EC 3.1.4.Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase: A group of related enzymes responsible for the endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose-content glycopeptides and GLYCOPROTEINS.Immunoelectrophoresis: A technique that combines protein electrophoresis and double immunodiffusion. In this procedure proteins are first separated by gel electrophoresis (usually agarose), then made visible by immunodiffusion of specific antibodies. A distinct elliptical precipitin arc results for each protein detectable by the antisera.Newspapers: Publications printed and distributed daily, weekly, or at some other regular and usually short interval, containing news, articles of opinion (as editorials and letters), features, advertising, and announcements of current interest. (Webster's 3d ed)Journalism, Medical: The collection, writing, and editing of current interest material on topics related to biomedicine for presentation through the mass media, including newspapers, magazines, radio, or television, usually for a public audience such as health care consumers.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Corynebacterium glutamicum: A species of gram-positive, asporogenous, non-pathogenic, soil bacteria that produces GLUTAMIC ACID.Corynebacterium: A genus of asporogenous bacteria that is widely distributed in nature. Its organisms appear as straight to slightly curved rods and are known to be human and animal parasites and pathogens.Kinetics: The rate dynamics in chemical or physical systems.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.beta-N-Acetyl-Galactosaminidase: A hexosiminidase that specifically hydrolyzes terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-beta-D-galactosaminides.Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor: Enzymes that catalyze the joining of glutamine-derived ammonia and another molecule. The linkage is in the form of a carbon-nitrogen bond. EC 6.3.5.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Receptors, Neuropeptide Y: Cell surface proteins that bind neuropeptide Y with high affinity and trigger intracellular changes which influence the behavior of cells.Rhabditoidea: A superfamily of nematodes of the order RHABDITIDA. Characteristics include an open tube stoma and an excretory system with lateral canals.Bacteriology: The study of the structure, growth, function, genetics, and reproduction of bacteria, and BACTERIAL INFECTIONS.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.
(1/982) An improved method for the structural profiling of keratan sulfates: analysis of keratan sulfates from brain and ovarian tumors.

A previously developed method for the structural fingerprinting of keratan sulfates (Brown et al., Glycobiology, 5, 311-317, 1995) has been adapted for use with oligosaccharides fluorescently labeled with 2-aminobenzoic acid following keratanase II digestion. The oligosaccharides are separated by high-pH anion-exchange chromatography on a Dionex AS4A-SC column. This methodology permits quantitative analysis of labeled oligosaccharides which can be detected at the sub-nanogram ( approximately 100 fmol) level. Satisfactory calibration of this method can be achieved using commercial keratan sulfate standards. Keratan sulfates from porcine brain phosphocan and human ovarian tumors have been examined using this methodology, and their structural features are discussed.  (+info)

(2/982) Effect of fasting on temporal variation in the nephrotoxicity of amphotericin B in rats.

Evidence for temporal variation in the nephrotoxicity of amphotericin B was recently reported in experimental animals. The role of food in these variations was determined by studying the effect of a short fasting period on the temporal variation in the renal toxicity of amphotericin B. Twenty-eight normally fed and 28 fasted female Sprague-Dawley rats were used. Food was available ad libitum to the fed rats, while the fasted animals were fasted 12 h before and 24 h after amphotericin B injection to minimize stress for the animals. Water was available ad libitum to both groups of rats, which were maintained on a 14-h light, 10-h dark regimen (light on at 0600 h). Renal toxicity was determined by comparing the levels of excretion of renal enzyme and the serum creatinine and blood urea nitrogen (BUN) levels at the time of the maximal (0700 h) or the minimal (1900 h) nephrotoxicity after the intraperitoneal administration of a single dose of dextrose (5%; control group) or amphotericin B (50 mg/kg of body weight; treated group) to the rats. The nephrotoxicities obtained after amphotericin B administration at both times of day were compared to the nephrotoxicities observed for time-matched controls. In fed animals, the 24-h urinary excretion of N-acetyl-beta-D-glucosaminidase and beta-galactosidase was significantly higher when amphotericin B was injected at 0700 and 1900 h. The excretion of these two enzymes was reduced significantly (P < 0.05) in fasting rats, and this effect was larger at 0700 h (P < 0.05) than at 1900 h. The serum creatinine level was also significantly higher (P < 0.05) in fed animals treated at 0700 h than in fed animals treated at 1900 h. Fasting reduced significantly (P < 0.05) the increase in the serum creatinine level, and this effect was larger in the animals treated at 0700 h. Similar data were obtained for BUN levels. Amphotericin B accumulation was significantly higher (P < 0.05) in the renal cortexes of fed rats than in those of fasted animals, but there was no difference according to the time of injection. These results demonstrated that fasting reduces the nephrotoxicity of amphotericin B and that food availability is of crucial importance in the temporal variation in the renal toxicity of amphotericin B in rats.  (+info)

(3/982) Endometrial lysosomal enzyme activity in normal cycling endometrium.

The objective of this study was to evaluate the possible role of four lysosomal enzymes in endometrial function and remodelling during the normal menstrual cycle by fluorimetric measurement (acid phosphatase, N-acetyl-beta-D-glucosaminidase, alpha-L-fucosidase and alpha-D-mannosidase). A prospective study was conducted of 45 endometrial biopsies obtained from women with normal menstrual cycles. Activity of all four enzymes was identified in human endometrium. Activity of acid phosphatase and N-acetyl-beta-D-glucosaminidase was relatively high, whilst that of alpha-L-fucosidase and alpha-D-mannosidase was low. There was no significant change in the activity of any of the four enzymes from the proliferative to the secretory phase of the cycle. This study suggests that the activity of these enzymes remains constant throughout a major portion of the normal cycle.  (+info)

(4/982) Immediate and early renal function after living donor transplantation.

BACKGROUND: In order to assess the immediate renal function after living donor transplantation, renal function was compared in eight renal allograft recipients and their living related kidney donors during the first 24 h after transplantation. METHODS: Substantial and comparable intraoperative volume loading with Ringer's acetate and mannitol was performed together with the administration of frusemide. Glomerular filtration rate (GFR) and effective renal plasma flow (ERPF) were estimated by the clearances of inulin and p-aminohippurane, respectively. Tubular reabsorptive function and injury were estimated from the clearance of lithium, the fractional excretion of sodium and the urinary excretion of N-acetyl-beta-glucosaminidase. RESULTS: One hour after completion of surgery, GFR (54 +/- 7 ml/min) and ERPF (294 +/- 35 ml/min) were only 30% lower in the grafts than in the remaining donor kidneys, increasing to similar levels within 3 h. Only minor tubular dysfunction and injury were revealed in the grafted kidneys, and these tended to normalize within 24 h. CONCLUSIONS: By the present transplantation procedure comprising short ischaemia time and substantial volume expansion combined with mannitol and frusemide administration, kidneys from living donors regain nearly normal function within a few hours after transplantation.  (+info)

(5/982) Active site characterization of the exo-N-acetyl-beta-D- glucosaminidase from thermotolerant Bacillus sp. NCIM 5120: involvement of tryptophan, histidine and carboxylate residues in catalytic activity.

The exo-N-acetyl-beta-d-glucosaminidase (EC 3.2.1.30) from thermotolerant Bacillus sp. NCIM 5120 is a homotetramer with a molecular mass of 240000 kDa. Chemical modification studies on the purified exo-N-acetyl-beta-d-glucosaminidase revealed the involvement of a single tryptophan, histidine and carboxylate, per monomer, in the catalytic activity of the enzyme. Spectral analysis and maintenance of total enzyme activities indicated that N-acetylglucosamine (competitive inhibitor) and p-nitrophenyl-N-acetyl-beta-d-glucosaminide (substrate) prevented the modification of a single essential tryptophan, histidine and carboxylate residue. Kinetic parameters of partially inactivated enzyme (by NBS/HNBB) showed the involvement of tryptophan in substrate binding while that of histidine (by photooxidation/DEPC) and carboxylate (by EDAC/WRK) in catalysis. The Bacillus sp. NCIM 5120 exo-N-acetyl-beta-d-glucosaminidase deviates from the reported N-acetyl-beta-d-glucosaminidases and beta-hexosaminidases that utilize anchimeric assistance in their hydrolytic mechanism.  (+info)

(6/982) Sanfilippo type B syndrome (mucopolysaccharidosis III B): allelic heterogeneity corresponds to the wide spectrum of clinical phenotypes.

Sanfilippo B syndrome (mucopolysaccharidosis IIIB, MPS IIIB) is caused by a deficiency of alpha-N-acetylglucosaminidase, a lysosomal enzyme involved in the degradation of heparan sulphate. Accumulation of the substrate in lysosomes leads to degeneration of the central nervous system with progressive dementia often combined with hyperactivity and aggressive behaviour. Age of onset and rate of progression vary considerably, whilst diagnosis is often delayed due to the absence of the pronounced skeletal changes observed in other mucopolysaccharidoses. Cloning of the gene and cDNA encoding alpha-N-acetylglucosaminidase enabled a study of the molecular basis of this syndrome. We were able to identify 31 mutations, 25 of them novel, and two polymorphisms in the 40 patients mostly of Australasian and Dutch origin included in this study. The observed allellic heterogeneity reflects the wide spectrum of clinical phenotypes reported for MPS IIIB patients. The majority of changes are missense mutations; also four nonsense and nine frameshift mutations caused by insertions or deletions were identified. Only five mutations were found in more than one patient and the observed frequencies are well below those observed for the common mutations in MPS IIIA. R643C and R297X each account for around 20% of MPS IIIB alleles in the Dutch patient group, whilst R297X, P521L, R565W and R626X each have a frequency of about 6% in Australasian patients. R643C seems to be a Dutch MPS IIIB allele and clearly confers the attenuated phenotype. One region of the gene shows a higher concentration of mutations, probably reflecting the instability of this area which contains a direct repeat. Several arginine residues seem to be 'hot-spots' for mutations, being affected by two or three individual base pair exchanges.  (+info)

(7/982) Effect of age on urinary excretion of N-acetyl-beta-D-glucosaminidase.

To examine the relationship between the concentrations of urinary NAG and age, we measured ratios of urinary N-acetyl-beta-D-glucosaminidase (NAG) to urinary creatinine (NAG index) in 137 healthy subjects, aged from 19 to 88 years. The study is also designed to evaluate the relationship between urinary NAG and blood pressure. The subjects were divided into 7 subgroups, according to their age (< 30, 30-39, 40-49, 50-59, 60-69, 70-79, 80 or more years). There was a positive correlation between NAG index and age (r = 0.36; P < 0.001). The regression equation relating NAG index (y) to age (x) was y = 0.065x + 0.97. The mean NAG indexes for the 7 subgroups divided by age were significantly different (P < 0.01). There was a positive correlation between NAG index and systolic blood pressure (r = 0.18; P < 0.05), but was not between diastolic blood pressure and NAG index. In multiple regression analysis, age and BUN significantly correlated with NAG index (r = 0.32; P < 0.01, r = 3.3; P = 0.07, respectively), although there was no correlation between systolic blood pressure and NAG index. This cross-sectional study showed a clear elevation in NAG index with age. The rate of elevation was 0.65 per decade. Urinary excretion of NAG may be unrelated to blood pressure.  (+info)

(8/982) A quantitative study of pinocytosis and lysosome function in experimentally induced lysosomal storage.

The highly pinocytic epithelial cells of the visceral yolk sac from 17.5-day rat conceptuses were used as a model in which to induce engorgement of the vacuolar system by direct accumulation of substances that are not hydrolysed by lysosomal enzymes. The ultra-structural appearances of these cells in pregnant animals that 24-48h before had received intraperitoneal injections of Triton WR-1339, polyvinylpyrrolidone, dextran or sucrose revealed gross abnormalities that were confined to the vacuolar system; in comparison with normal tissue the number, and in some cases the size, of vacuoles was increased, leading to close packing within the apical cytoplasm and distortion of the normal rounded shape. By culturing yolk sacs in vitro, rates of ingestion of 125I-labelled polyvinylpyrrolidone and of 125I-labelled bovine serum albumin were determined, together with the rate of digestion of the labelled protein. The rates of exocytosis of 125I-labelled polyvinylpyrrolidone and of lysosomal enzymes were also determined. No significant differences between normal and highly vacuolated tissues were found. Apparently marked vacuolation of these cells by these agents is without significant effect on pinocytosis, exocytosis or intralysosomal proteolysis.  (+info)

*  Alpha-N-acetylglucosaminidase
... (EC 3.2.1.50, alpha-acetylglucosaminidase, N-acetyl-alpha-D-glucosaminidase, N-acetyl-alpha- ... von Figura, K. (1977). "Human α-N-acetylglucosaminidase. 1. Purification and properties". Eur. J. Biochem. 80: 523-533. doi: ... von Figura, K. (1977). "Human α-N-acetylglucosaminidase. 2. Activity towards natural substrates and multiple recognition forms ... Weissmann, B.; Rowen, G.; Marshall, J.; Friederici, D. (1967). "Mammalian α-acetylglucosaminidase. Enzymic properties, tissue ...
*  Beta-aspartyl-N-acetylglucosaminidase
In enzymology, a beta-aspartyl-N-acetylglucosaminidase (EC 3.2.2.11) is an enzyme that catalyzes the chemical reaction 1-beta- ... Eylar EH; Murakami M (1966). "beta-Aspartyl-N-acetylglucosaminidase from epididymis". Methods Enzymol. Methods in Enzymology. 8 ...
*  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 ... Other names in common use include alpha-N-acetylglucosaminyl phosphodiesterase, lysosomal alpha-N-acetylglucosaminidase, ... phosphodiester glycosidase, alpha-N-acetyl-D-glucosamine-1-phosphodiester, N-acetylglucosaminidase, 2-acetamido-2-deoxy-alpha-D ...
*  Helge Stormorken
Further evidence of a hyperactive ?-N-acetylglucosaminidase-producing allele". Clinical Genetics. 41 (5): 243-247. doi:10.1111/ ...
*  NAGLU
N-acetylglucosaminidase, alpha is a protein that in humans is encoded by the NAGLU gene. This gene encodes an enzyme that ... N-acetylglucosaminidase, alpha". Weber B, Blanch L, Clements PR, Scott HS, Hopwood JJ (June 1996). "Cloning and expression of ... "Purification and partial characterization of alpha-N-acetylglucosaminidase from human liver". Journal of Biochemistry. 110 (5 ...
*  SGSH
... alpha-N-acetylglucosaminidase (type B; MIM 252920); acetyl CoA:alpha-glucosaminide acetyltransferase (type C; MIM 252930); and ...
*  Cortical granule
N-Acetylglucosaminidase: Experimentally found within mouse cortical granules, N-Acetylglucosaminidase is a glycosidase that ... Therefore, N-Acetylglucosaminidase contributes to polyspermy prevention. p32: The name, p32, refers to the protein's molecular ...
*  NAGPA
N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase is an enzyme that in humans is encoded by the NAGPA gene. ... "Entrez Gene: NAGPA N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase". Lee JK, Pierce M (1995). "Purification ... "Purification and characterization of human lymphoblast N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase". ... and functional expression of two splice forms of human N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase". J ...
*  Streptomyces plicatus
... produces endo-β-N-acetylglucosaminidase mithramycin, amicetin, bamicetin and plicacetin. ., Aghighi S ... "High-level expression of endo-β-N-acetylglucosaminidase H from Streptomyces plicatus in Pichia pastoris and its application for ...
*  Mucopolysaccharidosis
Sanfilippo B is caused by the missing or deficient enzyme alpha-N-acetylglucosaminidase. Sanfilippo C results from the missing ...
*  Beta-N-acetylgalactosaminidase
... β-N-acetylglucosaminidase, and β-N-acetylgalactosaminidase from calf brain". Biochemistry. 6: 2775-2782. doi:10.1021/ ...
*  MGEA5
... cytosolic beta-N-acetylglucosaminidase from human brain". J. Biol. Chem. 276 (13): 9838-45. doi:10.1074/jbc.M010420200. PMID ... "Analysis of MGEA5 on 10q24.1-q24.3 encoding the beta-O-linked N-acetylglucosaminidase as a candidate gene for type 2 diabetes ... a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase". Biochem. Biophys. Res. Commun. 283 (3): 634-40. doi:10.1006/ ... further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase". J. Biol. Chem. 277 (3): 1755-61. ...
*  PNGase F
Tachibana Y, Yamashita K, Kobata A (1982). "Substrate specificity of mammalian endo-beta-N-acetylglucosaminidase: study with ...
*  Endoglycosidase H
... endo-beta-N-acetylglucosaminidase D, endo-beta-N-acetylglucosaminidase F, endo-beta-N-acetylglucosaminidase H, endo-beta-N- ... di-N-acetylchitobiosyl beta-N-acetylglucosaminidase, endo-beta-acetylglucosaminidase, endo-beta-(1->4)-N-acetylglucosaminidase ... Chien, S.; Weinburg, R.; Li, S.; Li, Y. (1977). "Endo-β-N-acetylglucosaminidase from fig latex". Biochem. Biophys. Res. Commun ... The enzyme Endoglycosidase H (EC 3.2.1.96, Endo-β-N-acetylglucosaminidase H, N,N'-diacetylchitobiosyl beta-N- ...
*  Glycoside hydrolase family 89
Alpha-N-acetylglucosaminidase is a lysosomal enzyme required for the stepwise degradation of heparan sulphate. Mutations on the ... Glycoside hydrolase family 89 CAZY GH_89 includes enzymes with α-N-acetylglucosaminidase EC 3.2.1.50 activity. The enzyme ... "Mouse model of Sanfilippo syndrome type B produced by targeted disruption of the gene encoding alpha-N-acetylglucosaminidase". ... alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B ...
*  Hexosaminidase
Frohwein YZ, Gatt S (September 1967). "Isolation of β-N-acetylhexosaminidase, β-N-acetylglucosaminidase, and β-N- ... cytosolic beta-N-acetylglucosaminidase from human brain". J. Biol. Chem. 276 (13): 9838-45. doi:10.1074/jbc.M010420200. PMID ... beta-N-acetylglucosaminidase, hexosaminidase A, N-acetylhexosaminidase, beta-D-hexosaminidase) is an enzyme involved in the ... for β-N-acetylglucosaminidase, β-N-acetylhexosaminidase and β-N-acetylgalactosaminidase". Biochem. J. 261 (3): 1059-60. PMC ...
*  Lysin
Functionally, five types of lysin catalytic domain can be distinguished: Endo-β-N-acetylglucosaminidase N-acetylmuramidase ( ... Endo-β-N-acetylglucosaminidase lysins cleave NAGs while N-acetylmuramidase lysins (lysozyme-like lysins) cleave NAMs. ...
*  Glycoside hydrolase family 73
... CAZY GH_73 includes peptidoglycan hydrolases with endo-β-N-acetylglucosaminidase specificity. ...
*  Glycoside hydrolase family 85
... enzymes have endo-beta-N-acetylglucosaminidase activity EC 3.2.1.96 (CAZY GH_85). These enzymes ...
*  Protein O-GlcNAcase
... cytosolic β-N-acetylglucosaminidase from human brain". J. Biol. Chem. 276: 9838-9845. doi:10.1074/jbc.M010420200. PMID 11148210 ... further characterization of the nucleocytoplasmic β-N-acetylglucosaminidase, O-GlcNAcase". J. Biol. Chem. 277 (3): 1755-1761. ...
*  Sanfilippo syndrome
The NAGLU gene, located on chromosome 17q21.2, encodes alpha-N-acetylglucosaminidase, deficiency of which results in MPS IIIB. ...
*  Penicillium oxalicum
... produces secalonic acid D, chitinase, oxalic acid, oxaline and β-N-acetylglucosaminidase and occurs ...
*  Carbohydrate-binding module
CBM32 modules are associated with catalytic modules such as sialidases, B-N-acetylglucosaminidases, α-N-acetylglucosaminidases ...
*  HSD17B1
... of a cosmid from a gene-rich region in 17q21 and characterization of a candidate gene for alpha-N-acetylglucosaminidase with ...
*  Chitinase
... s (EC 3.2.1.14, chitodextrinase, 1,4-beta-poly-N-acetylglucosaminidase, poly-beta-glucosaminidase, beta-1,4-poly-N- ...
Mucopolysaccharidosis Type Iiib: Disease Bioinformatics: Novus Biologicals  Mucopolysaccharidosis Type Iiib: Disease Bioinformatics: Novus Biologicals
Mucopolysaccharidosis Type Iiib is also known as Alpha-n-acetylglucosaminidase Deficiency, Mps Iii B, Mps Iiib, N-acetyl-alpha- ...
more infohttps://www.novusbio.com/diseases/mucopolysaccharidosis-type-iiib
Expression of O-linked N-acetylglucosamine modified proteins and produ by Octavia Y. Goodwin  "Expression of O-linked N-acetylglucosamine modified proteins and produ" by Octavia Y. Goodwin
This was the first evidence that â-N-acetylglucosaminidase (NagZ), an E. coli enzyme, cleaves O-GlcNAc from proteins in vivo. ... O-(2-acetamido-2-dexoy-dglucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), a â-N-acetylglucosaminidase inhibitor, was added ... This was the first evidence that â-N-acetylglucosaminidase (NagZ), an E. coli enzyme, cleaves O-GlcNAc from proteins in vivo. ... O-(2-acetamido-2-dexoy-dglucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), a â-N-acetylglucosaminidase inhibitor, was added ...
more infohttps://digitalcommons.lsu.edu/gradschool_dissertations/3325/
Alpha-N-acetylglucosaminidase - Wikipedia  Alpha-N-acetylglucosaminidase - Wikipedia
Alpha-N-acetylglucosaminidase (EC 3.2.1.50, alpha-acetylglucosaminidase, N-acetyl-alpha-D-glucosaminidase, N-acetyl-alpha- ... von Figura, K. (1977). "Human α-N-acetylglucosaminidase. 1. Purification and properties". Eur. J. Biochem. 80: 523-533. doi: ... von Figura, K. (1977). "Human α-N-acetylglucosaminidase. 2. Activity towards natural substrates and multiple recognition forms ... Weissmann, B.; Rowen, G.; Marshall, J.; Friederici, D. (1967). "Mammalian α-acetylglucosaminidase. Enzymic properties, tissue ...
more infohttps://en.wikipedia.org/wiki/Alpha-N-acetylglucosaminidase
Beta-aspartyl-N-acetylglucosaminidase - Wikipedia  Beta-aspartyl-N-acetylglucosaminidase - Wikipedia
In enzymology, a beta-aspartyl-N-acetylglucosaminidase (EC 3.2.2.11) is an enzyme that catalyzes the chemical reaction 1-beta- ... Eylar EH; Murakami M (1966). "beta-Aspartyl-N-acetylglucosaminidase from epididymis". Methods Enzymol. Methods in Enzymology. 8 ...
more infohttps://en.wikipedia.org/wiki/Beta-aspartyl-N-acetylglucosaminidase
Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis.  - PubMed - NCBI  Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis. - PubMed - NCBI
Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis.. Huard C1, Miranda G, Wessner F, ... Though showing sequence similarity with enterococcal muramidase, AcmB has N-acetylglucosaminidase specificity. The acmB gene ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/12634338?dopt=Abstract
N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase activity Antibodies | Invitrogen
                       
   ...  N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase activity Antibodies | Invitrogen ...
Antibodies for proteins involved in N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase activity pathways, ... Antibodies for proteins involved in N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase activity pathways; ...
more infohttps://www.thermofisher.com/antibody/primary/panther/N-acetylglucosamine-1-phosphodiester%20alpha-N-acetylglucosaminidase%20activity
Mutants of Mucor hiemalis endo-beta-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities....  Mutants of Mucor hiemalis endo-beta-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities....
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase/chemistry*. *Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase/ ... Endo-beta-N-acetylglucosaminidase from Mucor hiemalis (Endo-M), a family 85 glycoside hydrolase, acts on the beta1,4 linkage of ... This is the first glycosynthase derived from endo-beta-N-acetylglucosaminidases that proceed via a substrate-assisted mechanism ... Mutants of Mucor hiemalis endo-beta-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities. ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/18096701
Catalytic Cycle of the N-Acetylglucosaminidase NagZ from Pseudomonas aeruginosa  Catalytic Cycle of the N-Acetylglucosaminidase NagZ from Pseudomonas aeruginosa
The N-acetylglucosaminidase NagZ of Pseudomonas aeruginosa catalyzes the first cytoplasmic step in recycling of muropeptides, ... The N-acetylglucosaminidase NagZ of Pseudomonas aeruginosa catalyzes the first cytoplasmic step in recycling of muropeptides, ... Catalytic Cycle of the N-Acetylglucosaminidase NagZ from Pseudomonas aeruginosa. 01-08-2017 ...
more infohttp://sebbm.es/web/es/divulgacion/articulo-mes/2261-catalytic-cycle-of-the-n-acetylglucosaminidase-nagz-from-pseudomonas-aeruginosa
N-Acetylglucosaminidase activity, a functional trait of chitin degradation, is regulated differentially within two orders of...  N-Acetylglucosaminidase activity, a functional trait of chitin degradation, is regulated differentially within two orders of...
N-Acetylglucosaminidase activity, a functional trait of chitin degradation, is regulated differentially within two orders of ... Because extracellular N-acetylglucosaminidase activity has been proposed as functional trait of chitin degradation, we screened ... Chitin degradation Chitinase N-Acetylglucosaminidase Functional trait Fungal phylogeny Electronic supplementary material. The ... Table S.2 Extracellular N-acetylglucosaminidase activity (pmol.ml-1.min-1) of ectomycorrhizal fungi with and without chitin in ...
more infohttps://link.springer.com/article/10.1007/s00572-018-0833-0
Endo-β-N-Acetylglucosaminidase catalysed glycosylation: tolerance of enzymes to structural variation of the glycosyl amino acid...  Endo-β-N-Acetylglucosaminidase catalysed glycosylation: tolerance of enzymes to structural variation of the glycosyl amino acid...
Endo-β-N-Acetylglucosaminidases (ENGases) are highly useful biocatalysts that can be used to synthetically access a wide ... Endo-β-N-Acetylglucosaminidases (ENGases) are highly useful biocatalysts that can be used to synthetically access a wide ... Endo-β-N-Acetylglucosaminidase catalysed glycosylation: tolerance of enzymes to structural variation of the glycosyl amino acid ... Endo-β-N-Acetylglucosaminidase catalysed glycosylation: tolerance of enzymes to structural variation of the glycosyl amino acid ...
more infohttp://pubs.rsc.org/en/Content/ArticleLanding/2013/OB/C3OB42104J?utm_source=feedburner&utm_medium=feed&utm_campaign=Feed%3A+rss%2FOB+%28RSC+-+Org.+Biomol.+Chem.+latest+articles%29
Insulin-like growth factor II peptide fusion enables uptake and lysosomal delivery of α-N-acetylglucosaminidase to...  Insulin-like growth factor II peptide fusion enables uptake and lysosomal delivery of α-N-acetylglucosaminidase to...
β-N-Acetylglucosaminidase from Streptococcus pneumoniae, recombinant, expressed in E. coli, buffered aqueous solution pricing ... β-N-Acetylglucosaminidase from Canavalia ensiformis (Jack bean), ammonium sulfate suspension, ≥15 units/mg protein pricing ... β-N-Acetylglucosaminidase from bovine kidney, ammonium sulfate suspension, 10-50 units/mg protein pricing ... Insulin-like growth factor II peptide fusion enables uptake and lysosomal delivery of α-N-acetylglucosaminidase to ...
more infohttps://www.sigmaaldrich.com/catalog/papers/24266751
Alpha-N-Acetylglucosaminidase (N-Acetyl-Alpha-Glucosaminidase or NAG or EC 3.2.1.50) - Pipeline Review, H1 2016 | Aug 16, 2016 ...  Alpha-N-Acetylglucosaminidase (N-Acetyl-Alpha-Glucosaminidase or NAG or EC 3.2.1.50) - Pipeline Review, H1 2016 | Aug 16, 2016 ...
Additionally, the report provides an overview of key players involved in Alpha-N-Acetylglucosaminidase (N-Acetyl-Alpha- ... The report provides comprehensive information on the Alpha-N-Acetylglucosaminidase (N-Acetyl-Alpha-Glucosaminidase or NAG or EC ... Alpha-N-Acetylglucosaminidase (N-Acetyl-Alpha-Glucosaminidase or NAG or EC 3.2.1.50) - Pipeline Review, H1 2016. 'The Report ... The report reviews latest news and deals related to Alpha-N-Acetylglucosaminidase (N-Acetyl-Alpha-Glucosaminidase or NAG or EC ...
more infohttp://www.sbwire.com/press-releases/alpha-n-acetylglucosaminidase-n-acetyl-alpha-glucosaminidase-or-nag-or-ec-32150-pipeline-review-h1-2016-714452.htm
Endo-β-N-acetylglucosaminidases from Infant Gut-associated Bifidobacteria Release Complex N-glycans from Human Milk...  Endo-β-N-acetylglucosaminidases from Infant Gut-associated Bifidobacteria Release Complex N-glycans from Human Milk...
Distribution of Endo-N-acetylglucosaminidase Gene Sequences in Bifidobacteria. Based on known endo-N-acetylglucosaminidase ... Endo-β-N-acetylglucosaminidases were identified in certain isolates of Bifidobacterium longum subsp. longum, B. longum subsp. ... 2001) Molecular cloning and expression of endo-β-N-acetylglucosaminidase D, which acts on the core structure of complex type ... 2000) Production of an endo-β-N-acetylglucosaminidase activity mediates growth of Enterococcus faecalis on a high-mannose-type ...
more infohttps://www.mcponline.org/content/11/9/775.long
2018-2025 Alpha N-Acetylglucosaminidase Report on Global and United States Market, Status and Forecast, by Players, Types and...  2018-2025 Alpha N-Acetylglucosaminidase Report on Global and United States Market, Status and Forecast, by Players, Types and...
2018-2025 Alpha N-Acetylglucosaminidase Report on Global and United States Market, Status and Forecast, by Players, Types and ... Global Alpha N-Acetylglucosaminidase Sales Market Report 2018. United States Alpha N-Acetylglucosaminidase Market Report 2018. ... 10.4 Alpha N-Acetylglucosaminidase Forecast by Type. 10.4.1 Global Alpha N-Acetylglucosaminidase Sales (K Pcs) and Revenue ( ... 2.1 Alpha N-Acetylglucosaminidase Product Overview. 2.2 Alpha N-Acetylglucosaminidase Market Segment by Type. 2.2.1 Lesinidase ...
more infohttp://www.rnrmarketresearch.com/2018-2025-alpha-n-acetylglucosaminidase-report-on-global-and-united-states-market-status-and-forecast-by-players-types-and-applications-market-report.html
Galactosyltransferase-dependent sialylation of complex and endo-N-acetylglucosaminidase H-treated core N-glycans in vitro.  -...  Galactosyltransferase-dependent sialylation of complex and endo-N-acetylglucosaminidase H-treated core N-glycans in vitro. -...
Galactosyltransferase-dependent sialylation of complex and endo-N-acetylglucosaminidase H-treated core N-glycans in vitro. ... Incorporation of sialic acid into endo-beta-N-acetylglucosaminidase H-treated oligomannose glycoproteins may be useful for in ... Incorporation of sialic acid into endo-beta-N-acetylglucosaminidase H-treated oligomannose glycoproteins may be useful for in ... Galactosyltransferase-dependent sialylation of complex and endo-N-acetylglucosaminidase H-treated core N-glycans in vitro. FEBS ...
more infohttps://www.zora.uzh.ch/id/eprint/632/
Carbohydrates - Analytical  Research - β-N-Acetyl-Glucosaminidase  Carbohydrates - Analytical Research - β-N-Acetyl-Glucosaminidase
Carbohydrates - β-N-Acetyl-Glucosaminidase. Megazyme's chromogenic substrates provide the most convenient methods for the assay ...
more infohttps://secure.megazyme.com/carbohydrates?activity=beta-n-acetyl-glucosaminidase&alt=1
HDCN:  Article by Navarro et al.
 Effects of <B>pentoxifylline</B> administration on urinary N-acetyl--
 glucosaminidase...  HDCN: Article by Navarro et al. Effects of <B>pentoxifylline</B> administration on urinary N-acetyl-- glucosaminidase...
Effects of pentoxifylline administration on urinary N-acetyl-- glucosaminidase excretion in type 2 diabetic patients: A short- ...
more infohttp://www.hdcn.com/03/008ajna.htm
N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase  N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
Compartment GO Terms for N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. Bounding membrane of organelle ... HCA RNA Cell Line for N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. ...
more infohttps://pharos.nih.gov/idg/targets/Q9UK23
N-Acetylglucosaminidase • QA-Bio Inc • Highest Purity • Highly Stable  N-Acetylglucosaminidase • QA-Bio Inc • Highest Purity • Highly Stable
N-acetylglucosaminidase cleaves all non-reducing terminal β-linked N-acetylglucosamine residues from complex carbohydrates and ... N-Acetylglucosaminidase. N-acetylglucosaminidase cleaves all non-reducing terminal β-linked N-acetylglucosamine residues from ... N-acetylglucosaminidase References. Clarke, V. A., N. Platt and T.D. Betters. Cloning and expression of the beta-N- ... N-acetylglucosaminidase cleaves all non-reducing terminal β-linked N-acetylglucosamine residues from complex carbohydrates and ...
more infohttps://www.qa-bio.com/product/n-acetylglucosaminidase/
  • O-(2-acetamido-2-dexoy-dglucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), a â-N-acetylglucosaminidase inhibitor, was added to the culture media and increased the production of O-GlcNAc-modified protein. (lsu.edu)
  • Mutants of Mucor hiemalis endo-beta-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities. (nih.gov)
  • Endo-beta-N-acetylglucosaminidase from Mucor hiemalis (Endo-M), a family 85 glycoside hydrolase, acts on the beta1,4 linkage of N,N'-diacetylchitobiose moiety in the N-linked glycans of glycoproteins and catalyzes not only the hydrolysis reaction but also the transglycosylation reaction that transfers the releasing sugar chain to an acceptor other than water to form a new glycosidic linkage. (nih.gov)
  • Purified beta-N-acetylglucosaminide beta(1-4)galactosyltransferase and partially purified beta-galactoside alpha(2-6)-sialyltransferase were used to elongate and terminate glycan chains of agalacto-ovalbumin and endo-beta-N-acetylglucosaminidase H-treated yeast invertase in vitro. (uzh.ch)
  • Incorporation of sialic acid into endo-beta-N-acetylglucosaminidase H-treated oligomannose glycoproteins may be useful for in vivo stabilization of these glycoproteins by preventing uptake in liver or reticuloendothelial cells. (uzh.ch)
  • In enzymology, a beta-aspartyl-N-acetylglucosaminidase (EC 3.2.2.11) is an enzyme that catalyzes the chemical reaction 1-beta-aspartyl-N-acetyl-D-glucosaminylamine + H2O ⇌ {\displaystyle \rightleftharpoons } L-asparagine + N-acetyl-D-glucosamine Thus, the two substrates of this enzyme are 1-beta-aspartyl-N-acetyl-D-glucosaminylamine and H2O, whereas its two products are L-asparagine and N-acetyl-D-glucosamine. (wikipedia.org)
  • The report provides comprehensive information on the Alpha-N-Acetylglucosaminidase (N-Acetyl-Alpha-Glucosaminidase or NAG or EC 3.2.1.50), targeted therapeutics, complete with analysis by indications, stage of development, mechanism of action (MoA), route of administration (RoA) and molecule type. (sbwire.com)
  • this report analyzes the top players in global and United States market, and splits the Alpha N-Acetylglucosaminidase market by product type and application/end industries. (rnrmarketresearch.com)