Amino Acid Metabolism, Part A, Volume 72, Advances in by Edited by: Daniel L. Purich, Daniel L. Purich

By Edited by: Daniel L. Purich, Daniel L. Purich

This ebook is a component A in a subseries entitled "Amino Acid Metabolism". issues partly A may be of quick curiosity to those that are generally considering amino acid assimilation and metabolism. Investigators drawn to enzyme mechanism and rules also will locate this quantity specially beneficial.

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Extra resources for Amino Acid Metabolism, Part A, Volume 72, Advances in Enzymology and Related Areas of Molecular Biology

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In that case, one must consider how nonsaturating physiologic levels of the various substrates act together to affect transpeptidase activity. The collective action of competitive inhibitors X, Y, and Z on a one-substrate enzyme exhibiting Michaelis-Menten behavior is given by the following equation: + where K,, Ky,and K , are inhibition constants. If the intracellular concentrationsof each end-product (in this case, X, Y, and Z) cannot permit saturation of the enzyme, then these agents behave collectively as virtual cumulative inhibitors.

We had planned to carry out later quench-flow studies on the formation of f3-amino-glutaryl-P, which would not be susceptible to cyclization and expulsion of Pi. Our findings were fully consistent with a random order of substrate addition. , 1977). H. ” These questions can often be answered by using Rose’s isotope trapping method, an approach that is based on Meister’s invention of a clever pulse-chase experiment. In an effort to build the case for an acyl-P intermediate, Krishnaswamy et al. (1962) incubated glutamine synthetase with [ ‘‘C]glutamate (the “pulse”) and ATP under conditions where they had scrupulously removed any ammonium ion (see Fig.

The amount of acyl-P formed in the above experiments corresponds to some 70% of the total enzyme concentration, and at first blush this appears to be rather large, especially when one considers that acyl-P compounds are substantially less stable than ATP. However, within the enzyme-bound state, the internal equilibrium Enz[ATPglutamate] = Enz[ADPglutamyl-PI may favor the acyl-P as a result of enzyme stabilizationof the bound intermediate. Arguing in favor of this interpretation are the data of Krishnaswamy et al.

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