Found 2 structures.
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1. Compound ID: 17028
Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141793,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_198,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 6614
Neustroev KN, Golubev AM, Firsov LM, Ibatullin FM, Protasevich II, Makarov AA "Effect of modification of carbohydrate component on properties of glucoamylase" -
FEBS Letters 316 (1993) 157-160
In this study, we investigated enzymatic deglycosylation of glucoamylase from Aspergillus awamori X 100/D27, a glycoprotein which has two N-linked and about forty short mannose-bearing O-linked sugars per molecule. O-Linked sugars were modified by treatment with α-mannosidase and N-linked sugars were removed using endo-β-N-acetylglucosaminidase F. Analysis of conformational changes following deglycosylation suggests that O-linked sugars essentially contribute to the stabilization of glucoamylase domains. Modification of the carbohydrate component by adding 1-deoxymannojirimycin to the culture medium induced inhibition of α-mannosidases involved in the processing, leading to a more complete glycosylation and, consequently, to a higher stability of the enzyme.
NCBI PubMed ID: 8420800Journal NLM ID: 0155157Publisher: Elsevier
Institutions: Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation
Methods: 13C NMR, GLC, MS, glucose oxidase method, enzymatic deglycosylation
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2. Compound ID: 17029
Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_137485,IEDB_141793,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_153220,IEDB_983930,IEDB_983931,SB_192,SB_198,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 6614
Neustroev KN, Golubev AM, Firsov LM, Ibatullin FM, Protasevich II, Makarov AA "Effect of modification of carbohydrate component on properties of glucoamylase" -
FEBS Letters 316 (1993) 157-160
In this study, we investigated enzymatic deglycosylation of glucoamylase from Aspergillus awamori X 100/D27, a glycoprotein which has two N-linked and about forty short mannose-bearing O-linked sugars per molecule. O-Linked sugars were modified by treatment with α-mannosidase and N-linked sugars were removed using endo-β-N-acetylglucosaminidase F. Analysis of conformational changes following deglycosylation suggests that O-linked sugars essentially contribute to the stabilization of glucoamylase domains. Modification of the carbohydrate component by adding 1-deoxymannojirimycin to the culture medium induced inhibition of α-mannosidases involved in the processing, leading to a more complete glycosylation and, consequently, to a higher stability of the enzyme.
NCBI PubMed ID: 8420800Journal NLM ID: 0155157Publisher: Elsevier
Institutions: Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation
Methods: 13C NMR, GLC, MS, glucose oxidase method, enzymatic deglycosylation
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