Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:EXPT00572 (Asn)
 11,732 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Heterogeneities of the two ovalbumin glycopeptides, (Man)5(GlcNAc)2Asn and (Man)6(GlcNAc)2Asn, were revealed by borate paper electrophoresis of oligosaccharide alcohols obtained from the glycopeptides by endo-beta-N-acetylglucosaminidase H digestion and NaB3H4 reduction. The structures of the major components of the oligosaccharides were determined by the combination of methylation analysis, acetolysis, and alpha-mannosidase digestion. Based on the results, the whole structures of the major components of (Man)5(GlcNAc)2Asn and (Man)6(GlcNAc)2Asn were elucidated as Manalpha1 leads to 6[Manalpha1 leads to 3]-Manalpha1 leads to 6[Manalpha1 leads to 3[Manbeta1 leads to 4GlcNAcbeta1 leads to 4GlcNAc leads to Asn and Manalpha1 leads to 6[Manalpha1 leads to 3]Manalpha1 leads to 6[Manalpha1 leads to 2Manalpha1 leads to 3]Manbeta1 leads to 4GlcNAcbeta1 leads to GlcNAc leads to Asn, respectively. Since endo-beta-N-acetylglucosamini dase D hydrolyzes (Man)5(GlcNAc)2Asn but not (Man)6(GlcNAc)2Asn, the presence of the unsubstituted alpha-mannosyl residue linked at the C-3 position of the terminal mannose of Manbeta1 leads to 4GlcNAcbeta1 leads to 4 GlcNAcAsn core must be essential for the action of the enzyme.
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PMID:Structural studies of two ovalbumin glycopeptides in relation to the endo-beta-N-acetylglucosaminidase specificity. 0 Mar 89

beta-D-Mannosidase (EC 3.2.1.25), a useful tool for the structural studies of heterosaccharide chains, has been isolated in a highly purified form from the fruiting bodies of the mushroom Polyporus sulfureus. This mushroom is unique among reported sources of this enzyme in that it has the advantage of being almost free of alpha-mannosidase activity. The purification procedure involves ammonium sulfate fractionation followed by Sephadex G-100 filtration and chromatography on columns of DEAE-cellulose and hydroxylapatite. The final enzyme preparation gives essentially a single band on disc gel electrophoresis. The purified enzyme liberates the beta-D-mannopyranosyl unit from various natural substrates such as the core glycopeptide, Man(GlcNAc)2-Asn isolated from ovalbumin, from Taka-amylase A, and from human alpha1-acid glycoprotein. It also hydrolyzes (Man)2-GlcNAc from the urine of an alpha-mannosidosis patient, 1,4-D-mannobiose and mannotriose isolated from ivory nut mannan, 4-O-beta-D-mannopyranosyl-L-rhamnose, 6-O-beta-D-mannopyranosyl-D-galactose and 4-O-beta-D-mannopyranosyl-N-acetylglucosamine. The molecular weight of this enzyme is estimated to be about 64,000 by gel filtration. For p-nitrophenyl-beta-D-mannopyranoside, the pH optimum is between 2.4 and 3.4 and the Km is 1.6 mM.
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PMID:beta-Mannosidase from the mushroom Polyporus sulfureus. 0 78

The effect os somatostatin (SS) and of its analogs D Trp 8-SS and Asn 5-SS was studied upon the external pancreatic secretion of the Rat after stimulation by 2 deoxy-D-glucose. The secretion of sodium and bicarbonate was similarly inhibited by all four peptides. The analog D Trp 8-SS was more effective in inhibiting pancreatic protein excretion.
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PMID:[Action of somatostatin and 3 analogs on external pancreatic secretion in the rat]. 10 39

The structures of the predominant high mannose oligosaccharides present in a human IgM myeloma protein (Patient Wa) have been determined. The IgM glycopeptides, produced by pronase digestion, were fractionated on DEAE-cellulonalysis shows that glycopeptide I contains Asn, Pro, Ala, Thr, and His and glycopeptide II contains Asn, Val, and Ser, which are the same amino acids found in the sequences around Asn 402 and Asn 563 respectively, to which high mannose oligosaccharides are attached in IgM (Patient Ou) (Putnman, F.W., Florent, G., Paul, C., Shinoda, T., and Shimizu, A. (1973) Science 182, 287-290). The high mannose glycopeptides in IgM (Wa) exhibit heterogeneity in the oligosaccharide portion. Structural analysis of the major oligosaccharides indicates that the simplest structure is: (see article of journal). The larger oligosaccharides present have additional mannose residues linked alpha 1 yields 2 to terminal mannose residues in the above structure. Glycopeptide I contains primarily Man5 and Man6 species, while glycopeptide II contains Man6 and Man8 species. The two Man6 oligosaccharides have different branching patterns.
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PMID:Structure of the high mannose oligosaccharides of a human IgM myeloma protein. I. The major oligosaccharides of the two high mannose glycopeptides. 10 97

The linkage of corneal keratan sulfate to protein has been investigated. After exhaustive digestion of bovine corneas with papain and pronase, a product was obtained in which aspartic acid was the predominant amino acid and constituted 59% of the total amino acids. A carbohydrate-protein linkage fragment was isolated from this preparation by a relatively simple procedure involving the following steps: (1) partial acid hydrolysis, adsorption of glycopeptides and other cationic material on Dowex 50-X2 (H+) and elution with 0.25 M HCl: (2) paper electrophoresis of the eluted fraction at pH 6.5 and pH 1.9; (3) paper chromatography; and (4) final purification by column chromatography on Aminex A"-5 resin. The structure of the linkage fragment was established as 2-acetamido-1-(L-beta-aspartamido)-1,2-dideoxy-beta-D-glucose (Asn-GlcNAc). Evidence for this structure was obtained from qualitative and quantitative analyses as well as from the migration characteristics in several chromatographic anc electrophoretic systems. Further support for the identity of the isolated compound was provided by treatment with beta-aspartyl N-acetylglucosyl-amine amidohydrolase which specifically cleaves Asn-GlcNAc or asparaginyl-oligosaccharides. It is concluded that corneal keratan sulfate is bound to protein via a N-glycosylamine linkage between N-acetylglucosamine and asparagine: this type of linkage is common to many glycoproteins.
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PMID:The linkage of corneal keratan sulfate to protein. 12 42

One neutral and two acidic glycoasparagines were isolated from the urine of patients with aspartylglycosylaminuria (AGU). The neutral one was identified as beta-Gal-(1 leads to 4)-beta-GlcNAc-Asn. The acidic ones were composed of 1 mole of sialic acid and 2 moles each of galactose and N-acetylglucosamine, attached to asparagine, and were isomeric with respect to the position of sialic acid attachment since they produced the same glycoasparagine on incubation with the neuraminidase [EC 3.2.1.18] from Clostridium perfringens. The structure of the resulting sialic acid-free glycoasparagine was determined to be beta-Gal-beta-GlcNAc-beta-Gal-(1 leads to 4)-beta-GlcNAc-Asn based mainly on the results of sequential enzymatic degradations.
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PMID:Characterization of one neutral and two acidic glycoasparagines isolated from the urine of patients with aspartylglycosylaminuria (AGU). 18 76

Studies in intact cells have shown the following processing reaction to occur during Asn-linked oligosaccharide biosynthesis (M, mannose; GlcNAc, N-acetylglucosamine): Formula: (See Text) We have identified a rat liver Golgi enzyme which catalyzes this reaction in vitro. This alpha-mannosidase has been purified 3,000 to 6,000-fold by subcellular fractionation, Triton X-100 solubilization, and ion exchange and hydroxylapatite chromatography. The purified enzyme has a pH optimum between 6.0 and 6.5 and a Km between 17 and 100 microM for a processing intermediate. The enzyme shows specificity for alpha 1,2-linked mannose residues. Structural analysis of the in vitro reaction products reveal that specific intermediates are formed in the conversion of the (Man)9GlcNAc oligosaccharide to the (Man)5GlcNAc oligosaccharide. Heat inactivation studies are consistent with the possibility that one enzyme activity is responsible for this conversion. The alpha 1,2-specific mannosidase described here appears to be distinct from two other rat liver Golgi alpha-mannosidase activities based on differential substrate specificity, inhibitor susceptibility, and detergent extractability.
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PMID:Purification and characterization of a rat liver Golgi alpha-mannosidase capable of processing asparagine-linked oligosaccharides. 50 Jun 65

The nonspecific alkaline phosphatase of yeast (Saccharomyces strain 1710) has been purified by ion exchange, hydrophobic, and affinity chromatography. This vacuolar enzyme has a molecular weight of 130,000 and is composed of subunits (probably of 66,000 molecular weight). It also has a small quantity of covalently associated carbohydrate; hydrolysis yielded mannose and glucosamine. The endo-beta-N-acetylglucosaminidase of Streptomyces plicatus released carbohydrate indicating that the latter was attached to protein through an N-acetylglucosaminylasparginyl bond. Synthesis of active alkaline phosphatase by yeast protoplasts is not depressed by tunicamycin, an inhibitor of dolichol-mediated protein glycosylation. Unlike the enzyme normally produced, the alkaline phosphatase which is formed in the presence of the antibiotic does not interact with concanavalin A and, therefore is deficient in or lacking carbohydrate. We infer that there is no regulatory link in yeast between the glycosylation of a protein and its synthesis. The fact that other Asn-GlcNAc-type glycoprotein enzymes of yeast such as acid phosphatase are not produced in their active forms by tunicamycin-treated protoplasts may mean that, as unglycosylated proteins, they cannot be correctly folded or processed. Protoplasts derepressed for phosphatase production contained substantial amounts of a second alkaline phosphatase which differed from the purified enzyme in substrate specificity, sensitivity to calcium, and reactivity with concanavalin A.
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PMID:Glycoprotein nature of yeast alkaline phosphatase. Formation of active enzyme in the presence of tunicamycin. 50 Jun 84

A lectin isolated from the seeds of sainfoin (Onobrychis viciifolia, Scop. var Eski) has been shown to be a glycoprotein containing 2.6% (w/w) neutral carbohydrate and 1.6% (w/w) glucosamine (Hapner, K.D. and Robbins, J.E. (1979) Biochim. Biophys. Acta 580, 186--197) A homogeneous glycopeptide accounting for 70% of the original glycoprotein carbohydrate was isolated from pronase digests of the lectin by gel filtration chromatography. Gas-liquid chromatographic and amino acid analyses showed the glycosyl portion to contain glucosamine, mannose, xylose and fucose in molar ratio to glycopeptide of 1.8 : 1.8 : 0.7 : 0.9. The amino acid sequence was determined as H2N-Ser-Asn(glycosyl)-glu-Thr-COOH. The glycosyl moiety was attached to the peptide through N-glycosidic linkage between asparagine and glucosamine.
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PMID:The glycosyl moiety of lectin from sainfoin (Onobrychis viciifolia, Scop.). 54 37

The structures of two glycoasparagines composed of one mole each of N-acetylneuraminic acid, galactose, N-acetylglucosamine, and asparagine were determined by periodate oxidation, enzymatic degradation, and methylation analysis. The structures were NANAalpha2 leads to 3Galbeta1 leads to 4GlcNAcbeta leads to Asn and NANAalpha2 leads to 6Galbeta1 leads to 4GlcNAcbeta leads to Asn, respectively.
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PMID:Structure of two glycoasparagines isolated from the urine of patients with aspartylglycosylaminuria (AGU). 59 15


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