Abstract
A uridylyltransferase (UTase) and a uridylyl removing enzyme (UR-enzyme) catalyze the uridylylation and deuridylylation, respectively, of Shapiro’s PII-regulatory protein. Uridylylated regulatory protein (PIID) stimulates the capacity of adenylyltransferase (ATase) to catalyze deadenylylation, whereas unmodified regulatory protein (PIIA) stimulates ATase catalyzed adenylylation of E. coli glutamine synthetase. Both uridylylation of PII and the adenylylation of glutamine synthetase are regulated by the concentrations of ATP, UTP, Pi, α-ketoglutarate, glutamine and the divalent cations, Mg2+ and Mn2+. The UTase, ATase, UR-enzyme, and the PII regulatory protein, together with the various metabolite effectors, constitute two oppositely directed cascade systems for the fine control of glutamine synthetase activity. The significance of these cascade systems in the control of glutamine metabolism is discussed.
Recipient of a U. S. Public Health Service Special Fellowship
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Abbreviations
- GS:
-
glutamine synthetase
- ATase:
-
adenylyltransferase
- UTase:
-
uridylyltransferase
- UR-enzyme:
-
uridylyl removing enzyme
- PIID :
-
uridylylated form of the PII regulatory protein
- PIIA :
-
unmodified form of the PII regulatory protein
- UR-UTase:
-
enzyme preparation containing both UR and UTase activities
- GLN:
-
glutanine
- α-KG:
-
α-ketoglutarate
- CP:
-
carbamyl-P
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Adler, S.P., Mangum, J.H., Magni, G., Stadtman, E.R. (1974). Uridylylation of the PII Regulatory Protein in Cascade Control of Escherichia coli Glutamine Synthetase. In: Metabolic Interconversion of Enzymes 1973. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80817-3_21
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DOI: https://doi.org/10.1007/978-3-642-80817-3_21
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