Glucose-6-phosphate isomerase, second

Many of the mechanistic aspects of glucose isomerase catalysed aldose-ketose interconversion have been under discussion for some time and are still not fully understood. By comparison with triose phosphate isomerase (TIM, EC 5.3.1.1) and glucose 6-phosphate isomerase (EC 5.3.1.9), the base-catalysed formation of an 1,2-enediol was invoked as the key step of the epimerisation based on the work of Rose and co-workers with tritium-labelled substrates [26]. An unexplained featme of the epimerisation process was that in contrast to isomerisations with triose phosphate isomerase no proton exchange with the medium could be observed with D-xylose isomerase, a fact that was attributed to the phosphate group of the former as a mediator for the exchange process [26]. Subsequently, additional important differences between triose phosphate isomerase and xylose isomerase were recognised. For example, D-xylose isomerase is appar-endy a very slow enzyme catalysing about five molecules per second per active site with an absolute requirement for divalent cations, while TIM does not need co-factors and operates at nearly 1000-fold the speed of D-xylose isomerase at... 

To summarize these observations First, the enzymes of this segment of the photosynthetic carbon reduction cycle are not controlled co-ordinately a single inductive step does not appear to affect the activity (and presumably the production) of these three enzymes in the same way. Second, the kinds of control mechanisms which appear to occur here are (1) a direct and prompt effect of illumination, reflected in the rapid increase in ribulose-diphosphate carboxylase activity, and (2) a more indirect kind of control, possibly involving induction of the other enzymes (e.g., ribose-phosphate isomerase) by small molecules produced in photosynthesis. Unfortunately, it has not been possible to demonstrate an increase in the level of either the isomerase or kinase by administration of glucose and some other carbohydrates to etiolated leaves in darkness. 

In the presence of excess phosphohexose isomerase and glucose-6-phos-phate dehydrogenase the rate of reduction of TPN is proportional to the rate of cleavage of fructose diphosphate. For cases when small, quantities of fructose diphosphate must be used, a second spectrophoto-metric assay, in which fructose diphosphate is regenerated, has been proposed 20). Fructose 6-phosphate is phosphorylated with ATP and phosphofructokinase, and the adenosine diphosphate (ADP) produced is measured with phosphoenolpyruvate and lactic dehydrogenase ... 

One molecule of glyceraldehyde-3-phosphate has already been produced by the aldolase reaction we now have a second molecule of glyceraldehyde-3-phosphate, produced by the triosephosphate isomerase reaction. The original molecule of glucose, which contains six carbon atoms, has now been converted to two molecules of glyceraldehyde-3-phosphate, each of which contains three carbon atoms. 

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