Cooperative Protection of Glucose-6-Phosphate Dehydrogenase by Ligands in Extracts from Wheat Grains

Fischer, Andreas; Salgó, András; Hildbrand, Markus; Feller, Urs (1992). Cooperative Protection of Glucose-6-Phosphate Dehydrogenase by Ligands in Extracts from Wheat Grains. Biochemie und Physiologie der Pflanzen, 188(5), pp. 295-303. Gustav Fischer Verlag 10.1016/S0015-3796(11)80125-3

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Protein stabilities can be influenced by interactions with low molecular weight compounds, Using glucose-6-phosphate dehydrogenase as a model protein in this context, we found that it was stabilized by low concentrations (below 5 mM) of inorganic phosphate or sulfate. The pyridine nucleotide NADP (one of the substrates in the enzyme reaction) already protected glucose-6-phosphate dehydrogenase activity at concentrations below 0.2 mM, whereas NAD was not effective. An excellent stabilization of glucose-6-phosphate dehydrogenase was achieved by the simultaneous addition of NADP and inorganic phosphate. Interactions of various ligands with different binding sites of the same enzyme can affect the susceptibility to proteolysis in a complex manner. Metabolic changes might influence selectively the catabolism of proteins in vivo by altering such interactions.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Other Institutions > Emeriti, Faculty of Science
08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS) > Plant nutrition (discontinued)
08 Faculty of Science > Department of Biology > Institute of Plant Sciences (IPS)

UniBE Contributor:

Feller, Urs

Subjects:

500 Science > 580 Plants (Botany)

ISSN:

0015-3796

Publisher:

Gustav Fischer Verlag

Language:

English

Submitter:

Peter Alfred von Ballmoos-Haas

Date Deposited:

22 Dec 2016 16:30

Last Modified:

05 Apr 2017 09:20

Publisher DOI:

10.1016/S0015-3796(11)80125-3

Uncontrolled Keywords:

Glucose-6-phosphate dehydrogenase, ligands, proteolysis, stabilization, Triticum aestivum L.

BORIS DOI:

10.7892/boris.91901

URI:

https://boris.unibe.ch/id/eprint/91901

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