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Taxonomic group: fungi / Ascomycota (Phylum: Ascomycota)

Publication DOI: 10.1006/prep.1998.0933
Journal NLM ID: 9101496
Publisher: Orlando, FL: Academic Press
Correspondence: glycoLab

cigb.edu.cu
Institutions: Bio-Industry Division, GlycoLab, Center for Genetic Engineering and Biotechnology, P.O. Box 6162, Havana, Cuba

We report the characterization of N-linked oligosaccharides on six foreign glycoproteins secreted from the methylotrophic yeast Pichia pastoris. These proteins included: a bacterial enzyme, Bacillus licheniformis α-amylase; three fungal enzymes, Saccharomyces cerevisiae invertase, Penicillium minioluteumdextranase, and Mucor pusillus aspartic protease; and two higher eukaryotic proteins, Boophilus microplus (tick) gut antigen and bovine enterokinase catalytic subunit. The carbohydrates on these proteins were observed to vary in size, with Man8GlcNAc2 and Man9GlcNAc2 structures being the most frequently observed species. Substantial amounts of shorter oligomannoside structures were present only on invertase, and longer structures (up to Man18GlcNAc2) were common on aspartic protease and enterokinase. Phosphorylated oligosaccharides were observed on one protein, aspartic protease. Unlike oligosaccharides on glycoproteins secreted fromS. cerevisiae, no terminal α1,3-linked mannosylation was observed on any of the six P. pastoris-secreted proteins. Changing the growth and induction medium from a minimal salt-based medium to a molasses-based medium had little effect on the size of the oligomannosides. From these results, it is apparent that most foreign proteins secreted from P. pastorisare not subjected to the extensive mannosylation (hyperglycosylation) that commonly occurs in proteins secreted from S. cerevisiae.

Structure type: oligomer
Location inside paper: fig. 3a
Aglycon: ANTS (8-amine-1,3,6-naphthalene trisulfonic acid)
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_187201,IEDB_429156,IEDB_548907,IEDB_857734,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85

Methods: partial acid hydrolysis, HPLC, enzymatic digestion, recombination techniques, fluorophore labeling, fluorophore-assisted carbohydrate electrophoresis
Enzymes that release or process the structure: α1,2-mannosidase (from Aspergillus saitoi)
Comments, role: glycopart of Bacillus licheniformis α-amylase; analytical product. D configurations of residues were assumed by CSDB staff.

Related record ID(s): 40808
NCBI Taxonomy refs (TaxIDs): 4922
Show glycosyltransferases

There are too many chemically distinct structures (~1536), so only one is shown:

aDManp(1-6)aDManp(1-3)[aDManp(1-3)[aDManp(1-6)]aDManp(1-6)]bDManp(1-4)[Ac(1-2)]?DGlcpN(1-1)[Ac(1-2)]?DGlcpN

CC(=O)N[C@H]1C(OC2O[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](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]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[C@@H](O)[C@H](O)[C@@H]4O)[C@@H]3O)[C@H](O)[C@H]2NC(C)=O)O[C@H](CO)[C@@H](O)[C@@H]1O

SVG MW SMILES 3D mol Ionize

Taxonomic group: fungi / Ascomycota (Phylum: Ascomycota)

Publication DOI: 10.1006/prep.1998.0933
Journal NLM ID: 9101496
Publisher: Orlando, FL: Academic Press
Correspondence: glycoLab

cigb.edu.cu
Institutions: Bio-Industry Division, GlycoLab, Center for Genetic Engineering and Biotechnology, P.O. Box 6162, Havana, Cuba

Structure type: oligomer
Location inside paper: fig. 3a
Aglycon: ANTS (8-amine-1,3,6-naphthalene trisulfonic acid)
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_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: partial acid hydrolysis, HPLC, enzymatic digestion, recombination techniques, fluorophore labeling, fluorophore-assisted carbohydrate electrophoresis
Enzymes that release or process the structure: α1,2-mannosidase (from Aspergillus saitoi)
Comments, role: glycopart of Bacillus licheniformis α-amylase; analytical product. D configurations of residues were assumed by CSDB staff.

Related record ID(s): 40544
NCBI Taxonomy refs (TaxIDs): 4922
Show glycosyltransferases

There are too many chemically distinct structures (~12288), so only one is shown:

aDManp(1-2)aDManp(1-2)[aDManp(1-6)]aDManp(1-3)[aDManp(1-3)[aDManp(1-2)aDManp(1-6)]aDManp(1-6)]bDManp(1-4)[Ac(1-2)]?DGlcpN(1-1)[Ac(1-2)]?DGlcpN

CC(=O)N[C@H]1C(OC2O[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]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O)[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)O[C@H](CO)[C@@H](O)[C@@H]1O

SVG MW SMILES 3D mol Ionize