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Effect of the Deletion of the (173–280) Fragment of the Inserted α-Helical Domain on the Functional Properties of АТР-Dependent Lon Protease from E. coli
Ist Teil von
Russian journal of bioorganic chemistry, 2018-09, Vol.44 (5), p.518-527
Ort / Verlag
Moscow: Pleiades Publishing
Erscheinungsjahr
2018
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
The effect of the coiled-coil (
CC
) region of the α-helical inserted domain of
Escherichia coli
Lon protease (Ec-Lon) on the functional activity of the enzyme has been characterized. A recombinant form des-
CC
(G5)-Lon in which the deleted
CC
fragment is replaced by a pentaglycine peptide has been obtained and investigated. It has been shown that the
CC
region is involved in the recognition of the nucleotide nature by the enzyme and the interaction of the enzyme with the protein substrate. It has been also established that the
CC
region is necessary for the formation and functioning of the ATPase and peptidase active centers, the occurrence of allosteric interactions between them, and for the implementation of proteolysis by a unique processive mechanism.