By Alton Meister
Ribonuclease P: An Enzyme with a Catalytic RNA Subunit (S. Altman).
rules of Escherichia coli Glutamine Synthetase (S. Rhee, et al.).
Glucose 6-Phosphatase: innovations of Membrane-Function courting (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 rules of the Glutamine-Dependent Carbamyl Phosphate Synthetase of Escherichia coli (A. Meister).
Cummulative Index, Vols.
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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 62
Cell. Biol. 6 , 1058 (1986). 54. , J . Biol. Chem. 260,5942 (1985). 55. S. , Cell 44, 213 (1986). 56. , Cell 44, 225 (1986). 36 SIDNEY ALTMAN 57. , in Subviral Pathogens of Plants and Animals: Viroids and Prions (K. J. ), pp. 235-263, Academic Press, New York (1985). 58. , Science 223,450 (1984). 59. , Biochemistry 24, 4785 (1985). 60. , Cell 49, 211 (1987). 61. , Cell 50, 9 (1987). 62. , Nature 328, 596 (1987). 63. ,Science 231, 470 (1986). 64. , Science 239, 1412 (1988). 65. ,in The Enzymes, Vol.
5 for Co(I1) system], the catalytic efficiency for Co(I1)-activated unadenylylated enzyme in catalyzing the biosynthetic reaction is only 20% of that activated by Mg(I1) (54). Metal-ion-binding study monitored by equilibrium dialysis with 54Mn(II)revealed the existence of three classes of divalent-cationbinding sites as judged by affinity differences (55). Saturation of the high-affhity site, nl, in each subunit with Mg(II), Mn(II), Ca(II), or Co(I1) is correlated to converting the relaxed enzyme to its active form (2,52,56-59).
Results of overall kinetic pattern analysis, with the exception of the product inhibition patterns obtained with glutamine as inhibitor, suggest that the reaction proceeds with an ordered ter-ter mechanism, with substrates binding in the order of MgATP, glutamate, and ammonia; the product release order is Pi, glutamine, and MgADP (76). The unexpected glutamine inhibition patterns were explained by the possibility that glutamine may bind to the substrate-free enzyme which then reacts with ATP to form a dead-end complex, or, alternatively, glutamine REGULATION OF ESCHERICHIA COLI GLUTAMINE SYNTHETASE 53 may bind to an allosteric site.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 62 by Alton Meister