CSDB: Search results

Taxonomic group: fungi / Ascomycota (Phylum: Ascomycota)

The structure was elucidated in this paper
NCBI PubMed ID: 2005096
Journal NLM ID: 2985121R
Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509

Asparagine-linked oligosaccharides are synthesized by transfer of Glc3Man9GlcNAc2 from dolichol pyrophosphate to nascent polypeptides. Assembly of the precursor proceeds by highly ordered sequential addition of mannose and glucose to form Glc3Man9GlcNAc2-P-P-dolichol. Yeast mutants in asparagine-linked glycosylation (alg), generated by an 3H-Man suicide technique, were assigned to eight complementation groups which define steps in oligosaccharide-lipid synthesis (Huffaker, T.C., and Robbins, P.W. (1982) J. Biol. Chem. 257, 3203-3210). Alg3 invertase oligosaccharides are resistant to endo-β-N-acetylglucosaminidase H, and the lipid-oligosaccharide pool yields Man5Glc-NAc2, suggesting its structure may be that from mammalian cells lacking Man-P-dolichol (Chapman, A., et al. (1980) J. Biol. Chem. 255, 4441-4446). To test this supposition, the endoplasmic reticulum form of invertase derepressed in alg3,sec18 yeast at 37 degrees C was isolated as a source of oligosaccharides whose processing beyond glucose and/or mannose trimming, if involved, would be prevented. Man8GlcNAc2 and Man5GlcNAc2 were released by peptide-N-glycosidase F from alg3,sec18 invertase in a 1:5 molar ratio. 1H NMR spectroscopy revealed Man8GlcNAc2 to be the α-1,2-mannosidase-trimming product described earlier (Byrd, J. C., Tarentino, A. L., Maley, F., Atkinson, P. H., and Trimble, R. B. (1982) J. Biol. Chem. 257, 14657-14666), while Man5GlcNAc2 was Man α-1, 2Man α-1,2Man α-1,3(Man α-1,6)Man β-1,4GlcNAc β-1,4GlcNAc. This provides a structural proof for the lipid-linked Man5GlcNAc2 originally proposed from enzymatic and chemical analyses of the radiolabeled mammalian precursor. Experimental evidence indicates that, unlike the mammalian cell mutants which are unable to synthesize Man-P-dolichol, alg3 yeast accumulate Man5GlcNAc2-P-P-dolichol due to a defective α-1,3-mannosyltransferase required for the next step in oligosaccharide-lipid elongation.

Structure type: oligomer
Location inside paper: Fig. 3A
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,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_153212,IEDB_153220,IEDB_164174,IEDB_187201,IEDB_187238,IEDB_187239,IEDB_429156,IEDB_540671,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85

Methods: 1H NMR, gel filtration, methylation analysis, PNGase F digestion, Smith-periodate oxidation
Biosynthesis and genetic data: genetic data
Comments, role: Parent molecule: invertase; invertase from alg3,sec18 strain was used

Related record ID(s): 111515, 117848, 136099
NCBI Taxonomy refs (TaxIDs): 4932
Reference(s) to other database(s): GTC:G08256MX, CCSD:50934, CBank-STR:19096
Show glycosyltransferases

There are 2 chemically distinct structures. Please, select:

CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO)[C@@H](O[C@@H]3O[C@H](CO[C@H]4O[C@H](CO[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H](O)[C@H](O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H]4O)[C@@H](O)[C@H](O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O)[C@@H]3O)[C@H](O)[C@H]2NC(C)=O)[C@@H]1O

SVG MW SMILES 3D mol Ionize

Structure type: oligomer
Location inside paper: Fig. 3B
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_540671,IEDB_548907,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85

Methods: 1H NMR, gel filtration, methylation analysis, PNGase F digestion, Smith-periodate oxidation
Biosynthesis and genetic data: genetic data
Comments, role: Parent molecule: invertase; invertase from alg3,sec18 strain was used

Related record ID(s): 136098, 136612, 136617
NCBI Taxonomy refs (TaxIDs): 4932
Reference(s) to other database(s): GTC:G11096GJ, CCSD:2847, CBank-STR:16486
Show glycosyltransferases

There are 2 chemically distinct structures. Please, select:

CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO)[C@@H](O[C@@H]3O[C@H](CO[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O)[C@@H](O)[C@H](O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]4O)[C@@H]3O)[C@H](O)[C@H]2NC(C)=O)[C@@H]1O

SVG MW SMILES 3D mol Ionize