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• W1985465025 startingPage "016006" @default.
• W1985465025 abstract "In the bacterium Escherichia coli, the enzyme glutamine synthetase (GS) converts ammonium into the amino acid glutamine. GS is principally active when the cell is experiencing nitrogen limitation, and its activity is regulated by a bicyclic covalent modification cascade. The advantages of this bicyclic-cascade architecture are poorly understood. We analyze a simple model of the GS cascade in comparison to other regulatory schemes and conclude that the bicyclic cascade is suboptimal for maintaining metabolic homeostasis of the free glutamine pool. Instead, we argue that the lag inherent in the covalent modification of GS slows the response to an ammonium shock and thereby allows GS to transiently detoxify the cell, while maintaining homeostasis over longer times." @default.
• W1985465025 created "2016-06-24" @default.
• W1985465025 creator A5043046053 @default.
• W1985465025 creator A5071133192 @default.
• W1985465025 date "2010-01-07" @default.
• W1985465025 modified "2023-09-25" @default.
• W1985465025 title "Modeling the role of covalent enzyme modification inEscherichia colinitrogen metabolism" @default.
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• W1985465025 doi "https://doi.org/10.1088/1478-3975/55/1/016006" @default.
• W1985465025 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3894576" @default.
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