Download Advances in Enzymology and Related Areas of Molecular by Alton Meister PDF

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 rules (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).

writer Index.

topic Index.

Cummulative Index, Vols.


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Additional info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 62

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Biol. 52, (1987). 10. , in Nucleases (S. Linn and R. ), pp. 243-274, Cold Spring Harbor Laboratory, New York (1982). 11. , Annu. Rev. Biochem. 45,605 (1976). 12. , Nature (London) New Biol. 229, 19 (1971). 13. , Nature (London) New Biol. 233, 35 (1971). 14. , J . Biol. Chem. 247,5243 (1972). 15. ,Cell 9, 101 (1976). 16. , J. Biol. Chem. 256, 5058 (1981). 17. , and Altman, S . , Proc. Natl. Acad. Sci. USA 75, 3717 (1978). 18. , in Transfer RNA: Biological Aspects (D. SOU, J. Abelson, and P. ), pp.

The molecules seen on edge show two layers of subunits, either as four spots (center) or, in general, two lines (bottom) when viewed exactly down a diameter between subunits. Magnification x 3,160,000. C. R. Stadtman, Biochemistry 7 2143-2152 (1968). Copyright 1968 American Chemical Society. quired for catalytic activity are bound to the C-domain of one polypeptide which makes up the larger portion of the catalytic center. The other surface of the catalytic center is derived from two beta strands of the N-domain of the adjacent subunit.

L - G +~ PPi + NHs Among these reactions, it is believed that only Reaction (l), also referred to as the biosynthetic reaction, is physiologically significant. Reaction (2) is used most often in assaying GS activity because one of the products, y-glutamylhydroxamate, is easily quantitated by colorimetric procedures (14). This reaction is commonly referred to as the y-glutamyl transfer reaction. Under certain circumstances, however, y-glutamyltransferase activity may not reflect the biosynthetic activity of the enzyme (15).

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