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Regulation of Glutamine Synthetase by Enzyme Catalyzed Structural Modification
Author(s) -
Shapiro Bennett M.
Publication year - 1970
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.197006701
Subject(s) - adenylylation , glutamine synthetase , glutamine , enzyme , biochemistry , chemistry , escherichia coli , biosynthesis , amino acid , gene
A highly sophisticated mechanism for the regulation of glutamine metabolism in Escherichia coli involves the modification of the enzyme glutamine synthetase by the covalent attachment and release of adenylyl residues. Separate enzymes catalyze the adenylylation and deadenylylation reactions, and these enzymes are reciprocally controlled by the state of nitrogen nutrition of the cell. The resultant structural alterations in glutamine synthetase enable it to change its catalytic potential greatly in response to varying cellular demands, in order to maintain nitrogen homeostasis.