role of carbohydrate in the glycoenzyme invertase of Neurospora crassa
Data obtained concerning the carbohydrate moieties of the glycoenzyme invertase (EC 3.2.1.26, beta-D-fructofuranoside fructohydrolase) from Neurospora crassa were consistent with a linkage of some carbohydrate chains by O-glycosidic bonds to serine and threonine residues; the possibility of N-glycos...
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Published in | Canadian journal of biochemistry Vol. 55; no. 3; pp. 249 - 256 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Canada
01.03.1977
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Subjects | |
Online Access | Get more information |
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Summary: | Data obtained concerning the carbohydrate moieties of the glycoenzyme invertase (EC 3.2.1.26, beta-D-fructofuranoside fructohydrolase) from Neurospora crassa were consistent with a linkage of some carbohydrate chains by O-glycosidic bonds to serine and threonine residues; the possibility of N-glycosylamine linkage of some of the carbohydrate to the amide group of asparagine is also indicated. The invertase was remarkably stable on storage at low temperatures. Oxidation of the carbohydrate residues in the enzyme by sodium periodate markedly affected the heat-stability of the enzyme. It is suggested that the carbohydrate moieties function as stabilizers of the tertiary structure of the glycoenzyme. |
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ISSN: | 0008-4018 |
DOI: | 10.1139/o77-035 |