By Edited by: Daniel L. Purich, Daniel L. Purich
This booklet is an element A in a subseries entitled "Amino Acid Metabolism". themes partially A can be of fast curiosity to people who are widely keen on amino acid assimilation and metabolism. Investigators drawn to enzyme mechanism and rules also will locate this quantity specifically worthy.
Read or Download Amino Acid Metabolism, Part A, Volume 72, Advances in Enzymology and Related Areas of Molecular Biology PDF
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Additional resources for Amino Acid Metabolism, Part A, Volume 72, Advances in Enzymology and Related Areas of Molecular Biology
Each feedback inhibitor was believed to bind at its own topologically distinct regulatory site on the synthetase. This model has become a standard entry in general biochemistry textbooks (Metzler, 1976; Voet and Voet, 1995;Matthews and van Holde, 1996; Stryer, 1988). Evidencefor the cumulative inhibition model was adduced chiefly from initial rate studies using both the enzyme’s biosynthetic and the y-glutamyl-transferase activities (described in Section A. 1). Before the adenylylation-deadenylylation cascade had been discovered, Woolfolk and Stadtman (1964; 1967) observed that raising the concentrations of any one of eight end-products to saturate the enzyme resulted in incomplete inhibition-a behavior that cannot be accounted for by classical competitive, noncompetitive, or uncompetitive inhibitor action.
1964) chemically synthesized (3-amino-glutarylP and demonstrated the enzymatic synthesis of P-amino-glutaramic acid (or P-glutamine)by ovine brain glutamine synthetase in the presence of ammonium ions. Likewise, they found that in the presence of hydroxylamine, p-amino-glutaryl-phosphatewas enzymatically transformed into P-amino-glutaryl-hydroxamate. Moreover, when the synthetic acyl-P was incubated with ADP and enzyme, ATP was formed. None of these reactions occurred in the absence of enzyme, and (3-aspartyl-Pwas completely ineffective in the above cited reactions.
29, 1951-1954 (1935). Krishnaswamy, P. , J . Biol. , 235, PC39 (1%0). Krisnaswamy, P. , J. Biol. , 237,2932-2940 (1%2). Levintow, L. , J. Biol. , 209, 265-269 (1954). Liaw, S. , and Eisenberg, D. , 4, 2358-2365 (1995). Liaw, S. , and Eisenberg, D. , Proc. Natl. Acad. Sci. USA, 90, 4996-5000 (1993). Liaw, S. , Biochemistry, 33, 11184-11188 (1994). , Curr. Top. Cell. , 27, 215-220 (1985). Manning, J. , Rowe, W. , Biochemistry, 8, 2681-2685 (1%9). 42 DANIEL L. PURICH Mathews, C. K. and van Holde, K.