Found 211 structures.
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1. Compound ID: 1478
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S-3)-+ S-3)-+
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S-3)-GlcpA-(1-4)-GlcpA-(1-4)-GlcpA-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn-(?--/-Asn-X-Thr/Ser- protein fragment/ |
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Structure type: oligomer
Aglycon: -Asn-X-Thr/Ser- protein fragment
Compound class: N-glycan
Contained glycoepitopes: IEDB_115136,IEDB_140630,IEDB_423153
The structure is contained in the following publication(s):
- Article ID: 468
Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" -
Glycobiology 14(8) (2004) 31R-42R
Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.
LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology
NCBI PubMed ID: 15044388Publication DOI: 10.1093/glycob/cwh064Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boka.ac.at
Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
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2. Compound ID: 4234
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Thr-(2-6)-b-D-ManpNAcA-(1-4)-b-D-GlcpNAc3NAcA-(1-3)-b-D-GlcpNAc1N-(1-4)-L-Asn |
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Structure type: oligomer
; 779
Compound class: N-glycan, S-layer glycan
The structure is contained in the following publication(s):
- Article ID: 1581
Voisin S, Houliston RS, Kelly J, Brisson JR, Watson D, Bardy SL, Jarrell KF, Logan SM "Identification and characterization of the unique N-linked glycan common to the flagellins and S-layer glycoprotein of Methanococcus voltae" -
Journal of Biological Chemistry 280(17) (2005) 16586-16593
The flagellum of Methanococcus voltae is composed of four structural flagellin proteins FlaA, FlaB1, FlaB2, and FlaB3. These proteins possess a total of 15 potential N-linked sequons (NX(S/T)) and show a mass shift on an SDS-polyacrylamide gel indicating significant post-translational modification. We describe here the structural characterization of the flagellin glycan from M. voltae using mass spectrometry to examine the proteolytic digests of the flagellin proteins in combination with NMR analysis of the purified glycan using a sensitive, cryogenically cooled probe. Nano-liquid chromatography-tandem mass spectrometry analysis of the proteolytic digests of the flagellin proteins revealed that they are post-translationally modified with a novel N-linked trisaccharide of mass 779 Da that is composed of three sugar residues with masses of 318, 258, and 203 Da, respectively. In every instance the glycan is attached to the peptide through the asparagine residue of a typical N-linked sequon. The glycan modification has been observed on 14 of the 15 sequon sites present on the four flagellin structural proteins. The novel glycan structure elucidated by NMR analysis was shown to be a trisaccharide composed of β-ManpNAcA6Thr-(1-4)-β-Glc-pNAc3NAcA-(1-3)-β-GlcpNAc linked to Asn. In addition, the same trisaccharide was identified on a tryptic peptide of the S-layer protein from this organism implicating a common N-linked glycosylation pathway.
NMR, structure, protein, glycan, glycosylation, NMR analysis, N-linked, glycoprotein, peptide, flagella, Flagellin, Methanococcus voltae, S-layer glycoprotein
NCBI PubMed ID: 15723834Publication DOI: 10.1074/jbc.M500329200Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: susan.logan@nrc-cnrc.gc.ca
Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A OR6, Canada, Department of Microbiology and Immunology, Queens University, Kingston, Ontario K7L 3N6, Canada
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, ESI-MS/MS, Western blotting, MALDI-TOF MS, NMR-1D, HPLC, enzymatic digestion, nLC-MS/MS
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3. 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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4. Compound ID: 7142
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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-(1-2)-Asn |
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Structure type: fragment of a bigger structure
Compound class: enterobacterial common antigen
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77
The structure is contained in the following publication(s):
- Article ID: 3238
Amin MN, Ishiwata A, Ito Y "Synthesis of asparagine-linked bacillosamine" -
Carbohydrate Research 341(11) (2006) 1922-1929
Various types of protein glycosylation have been identified from prokaryotes. Recent investigations have revealed the presence of N-linked glycoproteins in the pathogenic bacterium, Campylobacter jejuni. The structure of this glycan is unique, consisting of 5 GalNAc and 1 Glc, in addition to 2,4-diacetamido-2,4,6-trideoxy-d-glucopyranose (bacillosamine; Bac), which is N-glycosidically linked to the side chain of asparagine (Asn). We synthesized Bac from a 2-azido-2-deoxy-d-galactose derivative, which was further converted to the Asn-linked form.
Campylobacter jejuni, bacillosamine, N-Linked glycoprotein
NCBI PubMed ID: 16697990Publication DOI: 10.1016/j.carres.2006.04.031Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: yukito@riken.jp
Institutions: RIKEN (The Institute of Physical and Chemical Research), Wako, Japan, Graduate School of Science and Engineering, Saitama University, Sakura-ku, Saitama 338-8570, Japan, CREST, Japan Science and Technology Agency (JST), Kawaguchi, Saitama 332-1102, Japan
Methods: chemical synthesis
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5. Compound ID: 16590
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a-D-Manp-(1-4)-+
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b-D-Glcp-(1-4)-b-D-S6Quip-(1-3)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc1N-(1-4)-Asn-(?--/Asn-peptide/
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a-D-Manp-(1-6)-+ |
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Structure type: oligomer
Aglycon: Asn-peptide
Compound class: N-glycan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_137340,IEDB_141807,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_151531,IEDB_152206,IEDB_983930,IEDB_983931,SB_192,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 6434
Notaro A, Zaretsky M, Molinaro A, De Castro C, Eichler J "N-glycosylation in Archaea: Unusual sugars and unique modifications" -
Carbohydrate Research 534 (2023) 108963
Archaea are microorganisms that comprise a distinct branch of the universal tree of life and which are best known as extremophiles, residing in a variety of environments characterized by harsh physical conditions. One seemingly universal trait of Archaea is the ability to perform N-glycosylation. At the same time, archaeal N-linked glycans present variety in terms of both composition and architecture not seen in the parallel eukaryal or bacterial processes. In this mini-review, many of the unique and unusual sugars found in archaeal N-linked glycans as identified by nuclear magnetic resonance spectroscopy are described.
nuclear magnetic resonance spectroscopy, glycan structure, archaea, N-glycosylation, Extremophiles
NCBI PubMed ID: 37890267Publication DOI: 10.1016/j.carres.2023.108963Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: J. Eichler
Institutions: Department of Agricultural Sciences, University of Napoli Federico II, Portici, Italy, Department of Life Sciences, Ben-Gurion University of the Negev, Beersheva, Israel, Department of Chemical Sciences, University of Napoli Federico II, Napoli, Italy
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6. Compound ID: 16828
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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)-a-D-GlcpNAc1N-(1-4)-L-Asn-(?--/protein/ |
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Structure type: oligomer
Aglycon: protein
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_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,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: 6542
Runge KW, Huffaker TC, Robbins PW "Two yeast mutations in the glucosylation steps of the asparagine glycosylation pathway" -
Journal of Biological Chemistry 259 (1984) 412-417
Two complementing mutations in lipid-linked oligosaccharide biosynthesis have been isolated following a [3H]mannose suicide enrichment. Rather than making the wild type precursor oligosaccharide, Glc3man9Glc-NA2-P-P-dolichol, the mutants, alg5-1 and alg6-1, accumulate Man9GlcNAc2-P-P-dolichol as their largest lipid-linked oligosaccharide in vivo and in vitro. When UDP-[3H]Glc was added to microsomal membranes of each mutant, neither could elongate Man9GlcNAc2-P-P-dolichol and only alg6-1 could synthesize dolichol-phosphoglucose. When dolicholphospho[3H]glucose was added to microsomes from alg5-1, alg6-1, or the parental strain, only alg5-1 and the parental strain made glucosylated lipid-linked oligosaccharides. These results indicate that alg5-1 cells are unable to synthesize dolichol phosphoglucose while alg6-1 cells are unable to transfer glucose from dolichol phosphoglucose to the unglucosylated lipid-linked oligosaccharide. We also present evidence that both mutants transfer Man9GlcNAc2 to protein.
NCBI PubMed ID: 6423630Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Methods: gel filtration, acid hydrolysis, enzymatic digestion, in vivo labeling, in vitro labeling, assay for utilization of dolichol phosphoglucose
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7. 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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8. 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 |
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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_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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9. 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 |
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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_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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10. 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 |
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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_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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11. 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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12. Compound ID: 17117
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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)-D-GlcpNAc1N-(1-2)-Subst-(?--/invertase protein/
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
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Structure type: oligomer
Aglycon: invertase protein
Trivial name: Man8GlcNAc2
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_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,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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13. Compound ID: 17118
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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-(1-3)-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)-D-GlcpNAc1N-(1-2)-Subst-(?--/invertase protein/
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
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Structure type: oligomer
Aglycon: invertase protein
Trivial name: Man9GlcNAc2
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_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_174840,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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14. Compound ID: 17119
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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)-D-GlcNAc1N-(1-2)-Subst-(?--/invertase protein/
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
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Structure type: oligomer
Aglycon: invertase protein
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_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_174840,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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15. 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)-+ |
| |
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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