By Edited by: Daniel L. Purich, Daniel L. Purich
This publication is an element A in a subseries entitled "Amino Acid Metabolism". subject matters partly A can be of fast curiosity to those that are greatly concerned about amino acid assimilation and metabolism. Investigators drawn to enzyme mechanism and law also will locate this quantity in particular helpful.
Read or Download Amino Acid Metabolism, Part A, Volume 72, Advances in Enzymology and Related Areas of Molecular Biology PDF
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Extra resources for Amino Acid Metabolism, Part A, Volume 72, Advances in Enzymology and Related Areas of Molecular Biology
Assuming that the substrates are completely extended when bound to the enzyme, active substrates were obtained when the circled hydrogens are substituted by a methyl group. These hydrogens lie behind the plane of the paper, and they most probably face outward from the enzyme-bound substrate toward is an alternative substrate the bulk solvent. L-cis- l-A~o-l,3-dicarboxycyclohexane for glutamate in the glutamine synthetase reaction. Note that the cyclohexane ring is connected by three successive methylenes that bridge the two replaceable (circled) hydrogen atoms in L-glutamate.
Well aware that y-glutamyl derivatives are far more susceptible to nonenzymatic cyclization, Krishnaswamy et al. (1962) went on to demonstrate that glutamine formed the pyrrolidone-carboxylate some 600 times more slowly than in the corresponding enzymic step observed in the above experiment. This observation allowed Meister (1962) to offer a scheme involving the mandatory participation of an acyl-P intermediate in the glutamine synthetase reaction. Remarkably, that scheme (now modified modestly, as shown in Fig.
This would be the case because any unbound [ 14C]glutamate would be diluted by the much larger pool of unlabeled glutamate, thereby assuring that the fraction of the diluted tracer y-glutamyl-hydroxamate would be minimal, even after multiple catalytic rounds. An important advantage gained by utilizing hydroxylamine, as opposed to ammonium ion, was that the ADVANCES IN THE ENZYMOLOGY OF GLUTAMINE SYNTHESIS 25 Figure 4. Isotope trapping evidence for the formation of the acyl-P intermediate in the glutamine synthetase reaction.