By Alton Meister
Ribonuclease P: An Enzyme with a Catalytic RNA Subunit (S. Altman).
legislation of Escherichia coli Glutamine Synthetase (S. Rhee, et al.).
Glucose 6-Phosphatase: innovations of Membrane-Function dating (K. Sukalski & R. Nordlie).
Chiral Phosphorothioates: Stereochemical research of Enzymatic Substitution at Phosphorus (P. Frey).
Serotonin and Peptide Immunoneuromodulators: fresh Discoveries and New principles (D. Silverman & M. Karnovsky).
The Phosphyglycerate Mutases (L. Fothergill-Gilmore & H. Watson).
Mechanism and legislation of the Glutamine-Dependent Carbamyl Phosphate Synthetase of Escherichia coli (A. Meister).
Cummulative Index, Vols.
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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 62
Copyright 1986 American Chemical Society (ref. 35). RIBONUCLEASE P 29 30 SIDNEY ALTMAN mechanism lies in the fate of the transition-state complex, which can lead to the formation of a 5’-phosphate group and the recocking of the active site for another round of catalysis. The origin of the hydroxyl group that acts as a nucleophile-attacking agent is not known: It may come from the surface of the enzyme or from the solution. e,, the stereochemistry of the phosphates at the site of bond cleavage before and after the reaction), as well as the nature of the attacking groups, are still unknown.
5 molar equivalent of Zn(I1) can bind to each subunit when Zn(I1) is present at the 10 pM concentration range (58). Under this condition, some Zn(I1) ions may bind to nl and n2 since Zn(II), at 1 mM concentration, can support y-glutamyltransferase activity of the unadenylylated enzyme up to 50% of the expected Mg(I1)-supported activity (56). + + D. TOPOGRAPHICAL ANALYSIS Various ATP analogs can be used to adenylylate GS to yield an adenylylated enzyme which shows pH profile, divalent-metal-ion requirement, catalytic properties, and inhibitor properties similar to REGULATION OF ESCHERICHIA COLI GLUTAMINE SYNTHETASE 49 those of naturally adenylylated enzyme (62-66).
Tyrosine-397, indicated by a red line in Fig. 2a, is located near the interface between two subunits and is close to the outer periphery of the hexameric ring. The linkage between the adenylyl group and the hydroxyl group of tyrosine is a phosphodiester bond. B). Deadenylylation reaction involves phosphorolysis of the AMP-Tyr bond to form ADP and the unadenylylated enzyme (44). Under physiological conditions in which the Mg(I1) concentration is high while the Mn(I1) is present in trace amounts, the adenylylated enzyme is inactive in catalyzing the biosynthesis of glutamine.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 62 by Alton Meister