By Alton Meister

ISBN-10: 0470123087

ISBN-13: 9780470123089

ISBN-10: 0471617709

ISBN-13: 9780471617709

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).

writer Index.

topic Index.

Cummulative Index, Vols.

1-62.Content:

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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 62

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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.

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Advances in Enzymology and Related Areas of Molecular Biology, Volume 62 by Alton Meister


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