Neustroev KN, Golubev AM, Firsov LM, Ibatullin FM, Protasevich II, Makarov AA Effect of modification of carbohydrate component on properties of glucoamylase FEBS Letters316 (1993)
157-160
The structure was elucidated in this paper NCBI PubMed ID:8420800 Journal NLM ID:0155157 Publisher: Elsevier Institutions: Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation
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.
Related record ID(s): 125758 NCBI Taxonomy refs (TaxIDs):105351 Reference(s) to other database(s): GTC:G33131BN, CCSD:26370, CBank-STR:3078 Show glycosyltransferases
There are 3 chemically distinct structures. Please, select:
Neustroev KN, Golubev AM, Firsov LM, Ibatullin FM, Protasevich II, Makarov AA Effect of modification of carbohydrate component on properties of glucoamylase FEBS Letters316 (1993)
157-160
The structure was elucidated in this paper NCBI PubMed ID:8420800 Journal NLM ID:0155157 Publisher: Elsevier Institutions: Petersburg Nuclear Physics Institute, Gatchina, St. Petersburg, Russian Federation
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.
Related record ID(s): 125757 NCBI Taxonomy refs (TaxIDs):105351 Reference(s) to other database(s): GTC:G77553QO, CCSD:25067, CBank-STR:4514 Show glycosyltransferases
There are 3 chemically distinct structures. Please, select:
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