Limited Proteolysis of Glucose Dehydrogenase fromBacillus megateriumby Proteinase K
- 1 January 1983
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 364 (2) , 839-844
- https://doi.org/10.1515/bchm2.1983.364.2.839
Abstract
Glucose dehydrogenase from B. megaterium is subjected to proteolysis with proteinase K. Upon proteolysis the enzyme is inactivated and the polypeptide chain is cleaved into 2 distinct fragments. These components designated as K-protein and K-peptide have MW of 26,000 and 3000 [daltons], respectively. Under native conditions the K-protein and K-peptide remain associated and the tetrameric structure of the proteolytically modified enzyme is preserved. The K-protein and K-peptide were isolated and characterized. The cleavage occurs in the C-terminal region of the polypeptide chain. -Leu Ala .dwnarw. Ser-Ser-Glu is proposed as the cleavage site.This publication has 7 references indexed in Scilit:
- Conservation of primary structure at the proteinase-sensitive site of fructose 1,6-bisphosphatasesArchives of Biochemistry and Biophysics, 1982
- Limited proteolysis of glutamine synthetase is inhibited by glutamate and by feedback inhibitors.Journal of Biological Chemistry, 1979
- Conformational and functional aspects of the reversible dissociation and denaturation of glucose dehydrogenaseBiochemistry, 1977
- The Sequence Determination of a Protein in a Micro Scale: The Sequence Analysis of Ribosomal Protein L34 ofEscherichia coliHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976
- D-Glucose Dehydrogenase from Bacillus megaterium M 1286: Purification, Properties and StructureHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1975
- Rabbit liver fructose 1,6-diphosphatase. Properties of the native enzyme and their modification by subtilisinArchives of Biochemistry and Biophysics, 1972
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951