Enzymes of glycogen mobilization in the photosynthetic procaryote,Anacystis nidulans |
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Authors: | Martin Lehmann Günter Wöber |
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Institution: | (1) Biochemie, Fachbereich Chemie der Philipps-Universität, Lahnberge, Postfach 1929, D-3550 Marburg/Lahn, Federal Republic of Germany |
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Abstract: | Glycogen, the principal storage compound of assimilatory products in Anacystis nidulans, is synthesized in the light and degraded in the dark. 14C-labelled glycogen and its radioactive limit dextrin obtained by phosphorylase action were used as substrates to identify enzymes involved in glycogen mobilization. A crude homogenate of cells kept in the dark contained the following enzymes: glycogen phosphorylase (EC 2.4.1.1.) that is firmly bound to glycogen, a debranching enzyme that hydrolyzes 1,6--glucosidic bonds, and an -glucosidase (EC 3.2.1.20). Other amylolytic enzymes were not detectable Using ion exchange chromatography on DEAE-cellulose, -glucosidase and the debranching enzyme could be partly separated from each other and completely from the phosphorylase-glycogen complex. On the basis of their known substrate specificities, the cooperation of these 3 enzymes is sufficient to account for the complete conversion of glycogen into glucose and glucose 1-phosphate. |
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Keywords: | Anacystis Debranching enzyme -Glucosidase" target="_blank">gif" alt="agr" align="BASELINE" BORDER="0">-Glucosidase Glycogen mobilization Glycogen phosphorylase Polysaccharide (reserve) |
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