Found 87 structures.
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1. Compound ID: 5690
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a-D-Manp-(1-3)-+
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a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_429156,IEDB_857734,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 2481
Sherman P, Soni R, Del Vedovo S, Neeser JR "Effect of oligomannoside-type glycopeptides in diarrheal disease of rabbits induced by Escherichia coli strain RDEC-1" -
FEMS Microbiology Letters 61 (1989) 121-125
Journal NLM ID: 7705721Publisher: Blackwell Publishing
- Article ID: 10350
Debray H, Wieruszeski JM, Strecker G "Structural analysis of the carbohydrate chains isolated from mistletoe (Viscum album) lectin I" -
Carbohydrate Research 236 (1992) 135-143
Two glycopeptide fractions prepared from mistletoe (Viscum album) lectin I by Pronase digestion were fractioned by affinity chromatography on a concanavalin A-Sepharose column. With 400-MHz 1H NMR spectroscopy, in conjunction with sugar analysis, the following oligosaccharide structures could be determined: two oligomannose-type glycans in the ratio 4:1, one containing six mannose and the other containing five mannose units, both with two 2-acetamido-2-deoxyglucose units. In addition, a mannotriosyl→N,N'-diacetylchitobiose glycan containing a xylosyl group and an α-fucosyl group (1→3)-linked to the 2-acetamido-2-deoxyglycosyl-1 residue, a common core element of many plant glycoproteins, was also observed.
NCBI PubMed ID: 1291047Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Laboratoire de Chimie Biologique, Unité Mixte de Recherche du CNRS No. 111, Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq, France
- Article ID: 10801
Shao MC, Sokolik CW, Wold F "Noncovalent neoglycoproteins" -
Book: Neoglycoconjugates: Preparation and Applications (1994) 225-249
Book NLM ID: 9435300Publisher: San Diego: Academic Press
Editors: Lee YC, Lee RT
Institutions: MetroWest Medical Center Framingham, MA, USA
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2. Compound ID: 16915
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-3)-+ |
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ | |
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153762,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_174840,IEDB_233377,IEDB_429156,IEDB_76933,IEDB_857734,IEDB_857735,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6579
Young NM, Johnston RAZ, Richards JC "Purification of the a-L-rhamnosidase of Penicillium decumbens and characterization of two glycopeptide components" -
Carbohydrate Research 191 (1989) 53-62
Journal NLM ID: 0043535Publisher: Elsevier
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3. Compound ID: 16988
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-3)-+ |
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_233377,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6603
Ballou L, Hernandez LM, Alvarado E, Ballou CE "Revision of the oligosaccharide structures of yeast carboxypeptidase Y" -
Proceedings of the National Academy of Sciences of the USA 87 (1990) 3368-3372
The N-linked oligosaccharides from baker's yeast carboxypeptidase Y were analyzed by 1H NMR and specific mannosidase digestion and found to be identical to those from the Saccharomyces cerevisiae mnn9 mutant bulk mannoprotein. The results support the view that the mnn mutants make oligosaccharides that are a true reflection of the normal biosynthetic pathway and confirm that a recently revised yeast oligosaccharide structure is applicable to wild-type mannoproteins.
NCBI PubMed ID: 2185468Journal NLM ID: 7505876Publisher: National Academy of Sciences
Institutions: Department of Biochemistry, University of California, Berkeley 94720
Methods: 1H NMR, gel filtration, enzyme digestion, anion-exchange HPLC
- Article ID: 10063
Neeser JR, Del Vedovo S, Mutsaers JHGM, Vliegenthart JFG "Structural analysis of the carbohydrate chains of legume storage proteins by 500-MHz 1H-NMR spectroscopy" -
Glycoconjugate Journal 2 (1985) 355-364
soybean, 1H-NMR spectroscopy, kidney bean, oligomannoside-type glycopeptide, plant glycoprotein
Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Methods: 1H NMR, GLC, enzymatic digestion, HPTLC
- Article ID: 10228
Sturm A, Bergwerff AA, Vliegenthart JFG "1H-NMR structural determination of the N-linked carbohydrate chains on glycopeptides obtained from the bean lectin phytohemagglutinin" -
European Journal of Biochemistry 204 (1992) 313-316
Phytohemagglutinin, the lectin of the common bean Phaseolus vulgaris, is a N-linked glycoprotein with one high-mannose-type and one xylose-containing oligosaccharide side chain per polypeptide. The high-mannose-type glycan is attached to Asn12 and the complex-type glycan to Asn60 [Sturm, A. & Chrispeels, M. J. (1986) Plant Physiol. 81, 320-322]. The structures of the oligosaccharides were elucidated from two glycopeptides obtained from the lectin by Pronase digestion, affinity chromatography on concanavalin-A--Sepharose and gel-filtration chromatography on a column of BioGel P-4. The N-linked glycan structures were investigated by 500-MHz 1H-NMR spectroscopy and were established to be: [formula; see text]
NCBI PubMed ID: 1740144Journal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Friedrich Miescher-Institute, Basel, Switzerland
Methods: 1H NMR
- Article ID: 10801
Shao MC, Sokolik CW, Wold F "Noncovalent neoglycoproteins" -
Book: Neoglycoconjugates: Preparation and Applications (1994) 225-249
Book NLM ID: 9435300Publisher: San Diego: Academic Press
Editors: Lee YC, Lee RT
Institutions: MetroWest Medical Center Framingham, MA, USA
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4. Compound ID: 16989
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a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_233377,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6603
Ballou L, Hernandez LM, Alvarado E, Ballou CE "Revision of the oligosaccharide structures of yeast carboxypeptidase Y" -
Proceedings of the National Academy of Sciences of the USA 87 (1990) 3368-3372
The N-linked oligosaccharides from baker's yeast carboxypeptidase Y were analyzed by 1H NMR and specific mannosidase digestion and found to be identical to those from the Saccharomyces cerevisiae mnn9 mutant bulk mannoprotein. The results support the view that the mnn mutants make oligosaccharides that are a true reflection of the normal biosynthetic pathway and confirm that a recently revised yeast oligosaccharide structure is applicable to wild-type mannoproteins.
NCBI PubMed ID: 2185468Journal NLM ID: 7505876Publisher: National Academy of Sciences
Institutions: Department of Biochemistry, University of California, Berkeley 94720
Methods: 1H NMR, gel filtration, enzyme digestion, anion-exchange HPLC
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5. Compound ID: 16990
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a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-+ |
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a-D-Manp-(1--P--6)--a-D-Manp-(1-6)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-2)-+ | |
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a-D-Manp-(1--P--6)--a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_144996,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_233377,IEDB_429156,IEDB_474450,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6603
Ballou L, Hernandez LM, Alvarado E, Ballou CE "Revision of the oligosaccharide structures of yeast carboxypeptidase Y" -
Proceedings of the National Academy of Sciences of the USA 87 (1990) 3368-3372
The N-linked oligosaccharides from baker's yeast carboxypeptidase Y were analyzed by 1H NMR and specific mannosidase digestion and found to be identical to those from the Saccharomyces cerevisiae mnn9 mutant bulk mannoprotein. The results support the view that the mnn mutants make oligosaccharides that are a true reflection of the normal biosynthetic pathway and confirm that a recently revised yeast oligosaccharide structure is applicable to wild-type mannoproteins.
NCBI PubMed ID: 2185468Journal NLM ID: 7505876Publisher: National Academy of Sciences
Institutions: Department of Biochemistry, University of California, Berkeley 94720
Methods: 1H NMR, gel filtration, enzyme digestion, anion-exchange HPLC
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6. Compound ID: 16991
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a-D-Manp-(1-3)-+
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a-D-Manp-(1--P--6)--+ |
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ |
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a-D-Manp-(1--P--6)--+ | |
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_144996,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_174840,IEDB_233377,IEDB_429156,IEDB_474450,IEDB_76933,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6603
Ballou L, Hernandez LM, Alvarado E, Ballou CE "Revision of the oligosaccharide structures of yeast carboxypeptidase Y" -
Proceedings of the National Academy of Sciences of the USA 87 (1990) 3368-3372
The N-linked oligosaccharides from baker's yeast carboxypeptidase Y were analyzed by 1H NMR and specific mannosidase digestion and found to be identical to those from the Saccharomyces cerevisiae mnn9 mutant bulk mannoprotein. The results support the view that the mnn mutants make oligosaccharides that are a true reflection of the normal biosynthetic pathway and confirm that a recently revised yeast oligosaccharide structure is applicable to wild-type mannoproteins.
NCBI PubMed ID: 2185468Journal NLM ID: 7505876Publisher: National Academy of Sciences
Institutions: Department of Biochemistry, University of California, Berkeley 94720
Methods: 1H NMR, gel filtration, enzyme digestion, anion-exchange HPLC
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7. Compound ID: 17120
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a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
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Structure type: oligomer
Trivial name: Man9GlcNAc2
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_233377,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6647
Nakanishi-Shindo Y, Nakayama K, Nakayama KI, Tanaka A, Toda Y, Jigami Y "Structure of the N-linked oligosaccharides that show the complete loss of a-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae" -
Journal of Biological Chemistry 268 (1993) 26338-26345
The periplasmic invertase was purified from Saccharomyces cerevisiae och1::LEU2 disruptant cells (delta och1), which have a defect in elongation of the outer chain attached to the N-linked core oligosaccharides (Nakayama, K., Nagasu, T., Shimma, Y., Kuromatsu, J., and Jigami, Y. (1992) EMBO J. 11, 2511-2519). Structural analysis of the pyridylaminated (PA) neutral oligosaccharides released by hydrazinolysis and N-acetylation confirmed that the och1 mutation causes a complete loss of the α-1,6-polymannose outer chain, although the PA oligosaccharides (Man9GlcNAc2-PA and Man10GlcNAc2-PA), in which one or two α-1,3-linked mannose(s) attached to the endoplasmic reticulumn (ER)-form core oligosaccharide (Man8GlcNAc2) were also detected. Analysis of the delta och1 mnn1 strain oligosaccharides released from total cell mannoprotein revealed that the delta och1 mnn1 mutant eliminates the α-1,3-mannose attached to the core and accumulates predominantly a single ER-form oligosaccharide species (Man8GlcNAc2), suggesting a potential use of this strain as a host cell to produce glycoproteins containing mammalian high mannose type oligosaccharides. The delta och1 mnn1 alg3 mutants accumulated Man5GlcNAc2 and Man8GlcNAc2 in total cell mannoprotein, confirming the lack of outer chain addition to the incomplete corelike oligosaccharide and the leaky phenotype of the alg3 mutation. All the results suggest that the OCH1 gene encodes an α-1,6-mannosyltransferase that is functional in the initiation of α-1,6-polymannose outer chain addition to the N-linked core oligosaccharide (Man5GlcNAc2 and Man8GlcNAc2) in yeast.
NCBI PubMed ID: 8253757Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: National Institute of Bioscience and Human Technology, Ibaraki, Japan
Methods: 1H NMR, gel filtration, SDS-PAGE, HPLC, enzymatic digestion, hydrazinolysis, partial acetolysis, pyridylamination, Fab-MS
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8. Compound ID: 17121
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-3)-+ |
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
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Structure type: oligomer
Trivial name: Man10GlcNAc2
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_174840,IEDB_233377,IEDB_429156,IEDB_76933,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6647
Nakanishi-Shindo Y, Nakayama K, Nakayama KI, Tanaka A, Toda Y, Jigami Y "Structure of the N-linked oligosaccharides that show the complete loss of a-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae" -
Journal of Biological Chemistry 268 (1993) 26338-26345
The periplasmic invertase was purified from Saccharomyces cerevisiae och1::LEU2 disruptant cells (delta och1), which have a defect in elongation of the outer chain attached to the N-linked core oligosaccharides (Nakayama, K., Nagasu, T., Shimma, Y., Kuromatsu, J., and Jigami, Y. (1992) EMBO J. 11, 2511-2519). Structural analysis of the pyridylaminated (PA) neutral oligosaccharides released by hydrazinolysis and N-acetylation confirmed that the och1 mutation causes a complete loss of the α-1,6-polymannose outer chain, although the PA oligosaccharides (Man9GlcNAc2-PA and Man10GlcNAc2-PA), in which one or two α-1,3-linked mannose(s) attached to the endoplasmic reticulumn (ER)-form core oligosaccharide (Man8GlcNAc2) were also detected. Analysis of the delta och1 mnn1 strain oligosaccharides released from total cell mannoprotein revealed that the delta och1 mnn1 mutant eliminates the α-1,3-mannose attached to the core and accumulates predominantly a single ER-form oligosaccharide species (Man8GlcNAc2), suggesting a potential use of this strain as a host cell to produce glycoproteins containing mammalian high mannose type oligosaccharides. The delta och1 mnn1 alg3 mutants accumulated Man5GlcNAc2 and Man8GlcNAc2 in total cell mannoprotein, confirming the lack of outer chain addition to the incomplete corelike oligosaccharide and the leaky phenotype of the alg3 mutation. All the results suggest that the OCH1 gene encodes an α-1,6-mannosyltransferase that is functional in the initiation of α-1,6-polymannose outer chain addition to the N-linked core oligosaccharide (Man5GlcNAc2 and Man8GlcNAc2) in yeast.
NCBI PubMed ID: 8253757Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: National Institute of Bioscience and Human Technology, Ibaraki, Japan
Methods: 1H NMR, gel filtration, SDS-PAGE, HPLC, enzymatic digestion, hydrazinolysis, partial acetolysis, pyridylamination, Fab-MS
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9. Compound ID: 17122
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a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
Show graphically |
Structure type: oligomer
Trivial name: Man10GlcNAc2
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_233377,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6647
Nakanishi-Shindo Y, Nakayama K, Nakayama KI, Tanaka A, Toda Y, Jigami Y "Structure of the N-linked oligosaccharides that show the complete loss of a-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae" -
Journal of Biological Chemistry 268 (1993) 26338-26345
The periplasmic invertase was purified from Saccharomyces cerevisiae och1::LEU2 disruptant cells (delta och1), which have a defect in elongation of the outer chain attached to the N-linked core oligosaccharides (Nakayama, K., Nagasu, T., Shimma, Y., Kuromatsu, J., and Jigami, Y. (1992) EMBO J. 11, 2511-2519). Structural analysis of the pyridylaminated (PA) neutral oligosaccharides released by hydrazinolysis and N-acetylation confirmed that the och1 mutation causes a complete loss of the α-1,6-polymannose outer chain, although the PA oligosaccharides (Man9GlcNAc2-PA and Man10GlcNAc2-PA), in which one or two α-1,3-linked mannose(s) attached to the endoplasmic reticulumn (ER)-form core oligosaccharide (Man8GlcNAc2) were also detected. Analysis of the delta och1 mnn1 strain oligosaccharides released from total cell mannoprotein revealed that the delta och1 mnn1 mutant eliminates the α-1,3-mannose attached to the core and accumulates predominantly a single ER-form oligosaccharide species (Man8GlcNAc2), suggesting a potential use of this strain as a host cell to produce glycoproteins containing mammalian high mannose type oligosaccharides. The delta och1 mnn1 alg3 mutants accumulated Man5GlcNAc2 and Man8GlcNAc2 in total cell mannoprotein, confirming the lack of outer chain addition to the incomplete corelike oligosaccharide and the leaky phenotype of the alg3 mutation. All the results suggest that the OCH1 gene encodes an α-1,6-mannosyltransferase that is functional in the initiation of α-1,6-polymannose outer chain addition to the N-linked core oligosaccharide (Man5GlcNAc2 and Man8GlcNAc2) in yeast.
NCBI PubMed ID: 8253757Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: National Institute of Bioscience and Human Technology, Ibaraki, Japan
Methods: 1H NMR, gel filtration, SDS-PAGE, HPLC, enzymatic digestion, hydrazinolysis, partial acetolysis, pyridylamination, Fab-MS
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10. Compound ID: 17123
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a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
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Structure type: oligomer
Trivial name: Man11GlcNAc2
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_174840,IEDB_233377,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6647
Nakanishi-Shindo Y, Nakayama K, Nakayama KI, Tanaka A, Toda Y, Jigami Y "Structure of the N-linked oligosaccharides that show the complete loss of a-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae" -
Journal of Biological Chemistry 268 (1993) 26338-26345
The periplasmic invertase was purified from Saccharomyces cerevisiae och1::LEU2 disruptant cells (delta och1), which have a defect in elongation of the outer chain attached to the N-linked core oligosaccharides (Nakayama, K., Nagasu, T., Shimma, Y., Kuromatsu, J., and Jigami, Y. (1992) EMBO J. 11, 2511-2519). Structural analysis of the pyridylaminated (PA) neutral oligosaccharides released by hydrazinolysis and N-acetylation confirmed that the och1 mutation causes a complete loss of the α-1,6-polymannose outer chain, although the PA oligosaccharides (Man9GlcNAc2-PA and Man10GlcNAc2-PA), in which one or two α-1,3-linked mannose(s) attached to the endoplasmic reticulumn (ER)-form core oligosaccharide (Man8GlcNAc2) were also detected. Analysis of the delta och1 mnn1 strain oligosaccharides released from total cell mannoprotein revealed that the delta och1 mnn1 mutant eliminates the α-1,3-mannose attached to the core and accumulates predominantly a single ER-form oligosaccharide species (Man8GlcNAc2), suggesting a potential use of this strain as a host cell to produce glycoproteins containing mammalian high mannose type oligosaccharides. The delta och1 mnn1 alg3 mutants accumulated Man5GlcNAc2 and Man8GlcNAc2 in total cell mannoprotein, confirming the lack of outer chain addition to the incomplete corelike oligosaccharide and the leaky phenotype of the alg3 mutation. All the results suggest that the OCH1 gene encodes an α-1,6-mannosyltransferase that is functional in the initiation of α-1,6-polymannose outer chain addition to the N-linked core oligosaccharide (Man5GlcNAc2 and Man8GlcNAc2) in yeast.
NCBI PubMed ID: 8253757Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: National Institute of Bioscience and Human Technology, Ibaraki, Japan
Methods: 1H NMR, gel filtration, SDS-PAGE, HPLC, enzymatic digestion, hydrazinolysis, partial acetolysis, pyridylamination, Fab-MS
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11. Compound ID: 17124
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a-D-Manp-(1-3)-+
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_174840,IEDB_233377,IEDB_429156,IEDB_76933,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6647
Nakanishi-Shindo Y, Nakayama K, Nakayama KI, Tanaka A, Toda Y, Jigami Y "Structure of the N-linked oligosaccharides that show the complete loss of a-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae" -
Journal of Biological Chemistry 268 (1993) 26338-26345
The periplasmic invertase was purified from Saccharomyces cerevisiae och1::LEU2 disruptant cells (delta och1), which have a defect in elongation of the outer chain attached to the N-linked core oligosaccharides (Nakayama, K., Nagasu, T., Shimma, Y., Kuromatsu, J., and Jigami, Y. (1992) EMBO J. 11, 2511-2519). Structural analysis of the pyridylaminated (PA) neutral oligosaccharides released by hydrazinolysis and N-acetylation confirmed that the och1 mutation causes a complete loss of the α-1,6-polymannose outer chain, although the PA oligosaccharides (Man9GlcNAc2-PA and Man10GlcNAc2-PA), in which one or two α-1,3-linked mannose(s) attached to the endoplasmic reticulumn (ER)-form core oligosaccharide (Man8GlcNAc2) were also detected. Analysis of the delta och1 mnn1 strain oligosaccharides released from total cell mannoprotein revealed that the delta och1 mnn1 mutant eliminates the α-1,3-mannose attached to the core and accumulates predominantly a single ER-form oligosaccharide species (Man8GlcNAc2), suggesting a potential use of this strain as a host cell to produce glycoproteins containing mammalian high mannose type oligosaccharides. The delta och1 mnn1 alg3 mutants accumulated Man5GlcNAc2 and Man8GlcNAc2 in total cell mannoprotein, confirming the lack of outer chain addition to the incomplete corelike oligosaccharide and the leaky phenotype of the alg3 mutation. All the results suggest that the OCH1 gene encodes an α-1,6-mannosyltransferase that is functional in the initiation of α-1,6-polymannose outer chain addition to the N-linked core oligosaccharide (Man5GlcNAc2 and Man8GlcNAc2) in yeast.
NCBI PubMed ID: 8253757Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: National Institute of Bioscience and Human Technology, Ibaraki, Japan
Methods: 1H NMR, gel filtration, SDS-PAGE, HPLC, enzymatic digestion, hydrazinolysis, partial acetolysis, pyridylamination, Fab-MS
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12. Compound ID: 17125
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a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ |
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{{{-a-D-Man-(1-6)-}}}/n=49-99/-a-D-Man-(1-6)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153762,IEDB_153763,IEDB_164174,IEDB_233377,IEDB_429156,IEDB_76933,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6647
Nakanishi-Shindo Y, Nakayama K, Nakayama KI, Tanaka A, Toda Y, Jigami Y "Structure of the N-linked oligosaccharides that show the complete loss of a-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae" -
Journal of Biological Chemistry 268 (1993) 26338-26345
The periplasmic invertase was purified from Saccharomyces cerevisiae och1::LEU2 disruptant cells (delta och1), which have a defect in elongation of the outer chain attached to the N-linked core oligosaccharides (Nakayama, K., Nagasu, T., Shimma, Y., Kuromatsu, J., and Jigami, Y. (1992) EMBO J. 11, 2511-2519). Structural analysis of the pyridylaminated (PA) neutral oligosaccharides released by hydrazinolysis and N-acetylation confirmed that the och1 mutation causes a complete loss of the α-1,6-polymannose outer chain, although the PA oligosaccharides (Man9GlcNAc2-PA and Man10GlcNAc2-PA), in which one or two α-1,3-linked mannose(s) attached to the endoplasmic reticulumn (ER)-form core oligosaccharide (Man8GlcNAc2) were also detected. Analysis of the delta och1 mnn1 strain oligosaccharides released from total cell mannoprotein revealed that the delta och1 mnn1 mutant eliminates the α-1,3-mannose attached to the core and accumulates predominantly a single ER-form oligosaccharide species (Man8GlcNAc2), suggesting a potential use of this strain as a host cell to produce glycoproteins containing mammalian high mannose type oligosaccharides. The delta och1 mnn1 alg3 mutants accumulated Man5GlcNAc2 and Man8GlcNAc2 in total cell mannoprotein, confirming the lack of outer chain addition to the incomplete corelike oligosaccharide and the leaky phenotype of the alg3 mutation. All the results suggest that the OCH1 gene encodes an α-1,6-mannosyltransferase that is functional in the initiation of α-1,6-polymannose outer chain addition to the N-linked core oligosaccharide (Man5GlcNAc2 and Man8GlcNAc2) in yeast.
NCBI PubMed ID: 8253757Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: National Institute of Bioscience and Human Technology, Ibaraki, Japan
Methods: 1H NMR, gel filtration, SDS-PAGE, HPLC, enzymatic digestion, hydrazinolysis, partial acetolysis, pyridylamination, Fab-MS
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13. Compound ID: 17173
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a-D-Manp-(1-3)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6685
Aleshin AE, Hoffmann C, Firsov LM, Honzatko RB "Refined crystal structures of glucoamylase from Aspergillus awamori var. X100" -
Journal of Molecular Biology 238 (1994) 575-591
The refined crystal structures of a proteolytic fragment of glucoamylase from Aspergillus awamori var. X100 have been determined at pH 6 and 4 to a resolution of 2.2 A and 2.4 A, respectively. The models include the equivalent of residues 1 to 471 of glucoamylase from Aspergillus niger and a complete interpretation of the solvent structure. The R-factors of the pH 6 and 4 structures are 0.14 and 0.12, respectively, with root-mean-square deviations of 0.014 A and 0.012 A from expected bondlengths. The enzyme has the general shape of a doughnut. The "hole" of the doughnut consists of a barrier of hydrophobic residues at the center, which separates two water-filled voids, one of which serves as the active site. Three clusters of water molecules extend laterally from the active site. One of the lateral clusters connects the deepest recess of the active site to the surface of the enzyme. The most significant difference in the pH 4 and 6 structures is the thermal parameter of water 500, the putative nucleophile in the hydrolysis of maltooligosaccharides. Water 500 is associated more tightly with the enzyme at pH 4 (the pH of optimum catalysis) than at pH 6. In contrast to water 500, Glu179, the putative catalytic acid of glucoamylase, retains the same conformation in both structures and is in an environment that would favor the ionized, rather than the acid form of the side-chain. Glycosyl chains of 5 and 8 sugar residues are linked to Asparagines 171 and 395, respectively. The conformations of the two glycosyl chains are similar, being superimposable on each other with a root-mean-square discrepancy of 1.9 A. The N-glycosyl chains hydrogen bond to the surface of the protein through their terminal sugars, but otherwise do not interact strongly with the enzyme. The structures have ten serine/threonine residues, to each of which is linked a single mannose sugar. The structure of the ten O-glycosylated residues taken together suggests a well-defined conformation for proteins that have extensive O-glycosylation of their polypeptide chain.
NCBI PubMed ID: 8176747Publication DOI: 10.1006/jmbi.1994.1316Journal NLM ID: 2985088RPublisher: Elsevier
Institutions: Department of Molecular, St Petersburg Nuclear Physics Institute, Russia
Methods: X-ray, SDS-PAGE
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14. Compound ID: 17175
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-6)-+ |
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a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
Show graphically |
Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_143632,IEDB_144983,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6685
Aleshin AE, Hoffmann C, Firsov LM, Honzatko RB "Refined crystal structures of glucoamylase from Aspergillus awamori var. X100" -
Journal of Molecular Biology 238 (1994) 575-591
The refined crystal structures of a proteolytic fragment of glucoamylase from Aspergillus awamori var. X100 have been determined at pH 6 and 4 to a resolution of 2.2 A and 2.4 A, respectively. The models include the equivalent of residues 1 to 471 of glucoamylase from Aspergillus niger and a complete interpretation of the solvent structure. The R-factors of the pH 6 and 4 structures are 0.14 and 0.12, respectively, with root-mean-square deviations of 0.014 A and 0.012 A from expected bondlengths. The enzyme has the general shape of a doughnut. The "hole" of the doughnut consists of a barrier of hydrophobic residues at the center, which separates two water-filled voids, one of which serves as the active site. Three clusters of water molecules extend laterally from the active site. One of the lateral clusters connects the deepest recess of the active site to the surface of the enzyme. The most significant difference in the pH 4 and 6 structures is the thermal parameter of water 500, the putative nucleophile in the hydrolysis of maltooligosaccharides. Water 500 is associated more tightly with the enzyme at pH 4 (the pH of optimum catalysis) than at pH 6. In contrast to water 500, Glu179, the putative catalytic acid of glucoamylase, retains the same conformation in both structures and is in an environment that would favor the ionized, rather than the acid form of the side-chain. Glycosyl chains of 5 and 8 sugar residues are linked to Asparagines 171 and 395, respectively. The conformations of the two glycosyl chains are similar, being superimposable on each other with a root-mean-square discrepancy of 1.9 A. The N-glycosyl chains hydrogen bond to the surface of the protein through their terminal sugars, but otherwise do not interact strongly with the enzyme. The structures have ten serine/threonine residues, to each of which is linked a single mannose sugar. The structure of the ten O-glycosylated residues taken together suggests a well-defined conformation for proteins that have extensive O-glycosylation of their polypeptide chain.
NCBI PubMed ID: 8176747Publication DOI: 10.1006/jmbi.1994.1316Journal NLM ID: 2985088RPublisher: Elsevier
Institutions: Department of Molecular, St Petersburg Nuclear Physics Institute, Russia
Methods: X-ray, SDS-PAGE
- Article ID: 6733
Akiba S, Yamamoto K, Kumagai H "Effects of size of carbohydrate chain on protease digestion of Aspergillus niger endo-b-1,4-glucanase" -
Bioscience, Biotechnology, and Biochemistry 59 (1995) 1048-1051
NCBI PubMed ID: 7612990Journal NLM ID: 9205717Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
- Article ID: 6812
Flores-Carreon A, Balcazar-Orozco R "Biosynthesis of glycoproteins in Candida albicans: Processing of a Man6-GlcNAc2-Asn oligosaccharide by membrane fractions" -
FEMS Microbiology Letters 110 (1993) 121-126
Journal NLM ID: 7705721Publisher: Blackwell Publishing
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15. Compound ID: 17190
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-+
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a-D-Glcp-(1-2)-a-D-Glcp-(1-3)-a-D-Glcp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn |
Show graphically |
Structure type: oligomer
Trivial name: Glc3Man9GlcNAc2
Compound class: N-glycan, high-mannose
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_149158,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_232584,IEDB_233377,IEDB_429156,IEDB_857734,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 6701
Orlean P "Dolichol phosphate mannose synthase is required in vivo for glycosyl phosphatidylinositol membrane anchoring, O mannosylation, and N glycosylation of protein in Saccharomyces cerevisiae" -
Molecular and Cellular Biology 10 (1990) 5796-5805
Glycosyl phosphatidylinositol (GPI) anchoring, N glycosylation, and O mannosylation of protein occur in the rough endoplasmic reticulum and involve transfer of precursor structures that contain mannose. Direct genetic evidence is presented that dolichol phosphate mannose (Dol-P-Man) synthase, which transfers mannose from GDPMan to the polyisoprenoid dolichol phosphate, is required in vivo for all three biosynthetic pathways leading to these covalent modifications of protein in yeast cells. Temperature-sensitive yeast mutants were isolated after in vitro mutagenesis of the yeast DPM1 gene. At the nonpermissive temperature of 37 degrees C, the dpm1 mutants were blocked in [2-3H]myo-inositol incorporation into protein and accumulated a lipid that could be radiolabeled with both [2-3H]myo-inositol and [2-3H]glucosamine and met existing criteria for an intermediate in GPI anchor biosynthesis. The likeliest explanation for these results is that Dol-P-Man donates the mannose residues needed for completion of the GPI anchor precursor lipid before it can be transferred to protein. Dol-P-Man synthase is also required in vivo for N glycosylation of protein, because (i) dpm1 cells were unable to make the full-length precursor Dol-PP-GlcNAc2Man9Glc3 and instead accumulated the intermediate Dol-PP-GlcNAc2Man5 in their pool of lipid-linked precursor oligosaccharides and (ii) truncated, endoglycosidase H-resistant oligosaccharides were transferred to the N-glycosylated protein invertase after a shift to 37 degrees C. Dol-P-Man synthase is also required in vivo for O mannosylation of protein, because chitinase, normally a 150-kDa O-mannosylated protein, showed a molecular size of 60 kDa, the size predicted for the unglycosylated protein, after shift of the dpm1 mutant to the nonpermissive temperature.
NCBI PubMed ID: 2146492Journal NLM ID: 8109087Publisher: American Society for Microbiology
Institutions: Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139
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Next 15 structure(s)
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