Aspartate can form arginosuccinate, which can then release a fumarate molecule. The fumarate can enter into the Krebs cycle and eventually the pathway can lead to gluconeogenesis. The arginine from the arginosuccinate can continue through the urea cycle.

Aspartate can form arginosuccinate, which can then release a fumarate molecule. The fumarate can enter into the Krebs cycle and eventually the pathway can lead to gluconeogenesis. The arginine from the arginosuccinate can continue through the urea cycle.

In order to linearize using a linkage, there needs to be an unbound carbon on the 1 position. However, sucrose is a linkage and doesn't have a carbon available to linearize in the 1 position. It isn't a reducing sugar and therefore cannot be linearized. All of the other sugars have their anomeric carbon located at the 1 position and all of them are reducing sugars that can be linearized.

In order to linearize using a linkage, there needs to be an unbound carbon on the 1 position. However, sucrose is a linkage and doesn't have a carbon available to linearize in the 1 position. It isn't a reducing sugar and therefore cannot be linearized. All of the other sugars have their anomeric carbon located at the 1 position and all of them are reducing sugars that can be linearized.

From the question stem, we are told that glucose-6-phosphate dehydrogenase oxidized glucose into another compound, and also produces a molecule of NADPH in the process. In order to determine the way in which this enzyme is likely to be regulated, it's important to consider feedback mechanics.

Since this enzyme is producing NADPH when it is turned on, we would expect this product to negatively regulate the enzyme via feedback inhibition. Moreover, since we know that is a reactant, we can correctly assume that having a high concentration of this will likely drive the reaction forward by turning the enzyme on. Thus, would be expected to allosterically activate this enzyme. Furthermore, the question stem tells us nothing about the unphosphorylated forms of these cofactors, therefore we have no way of knowing how many NADH or affects this enzyme, if they do at all.

From the question stem, we are told that glucose-6-phosphate dehydrogenase oxidized glucose into another compound, and also produces a molecule of NADPH in the process. In order to determine the way in which this enzyme is likely to be regulated, it's important to consider feedback mechanics.

Since this enzyme is producing NADPH when it is turned on, we would expect this product to negatively regulate the enzyme via feedback inhibition. Moreover, since we know that is a reactant, we can correctly assume that having a high concentration of this will likely drive the reaction forward by turning the enzyme on. Thus, would be expected to allosterically activate this enzyme. Furthermore, the question stem tells us nothing about the unphosphorylated forms of these cofactors, therefore we have no way of knowing how many NADH or affects this enzyme, if they do at all.

From the question stem, we are shown the reaction in which glucose-6-phosphate is transformed into ribulose-5-phosphate. We are then asked to determine which type of reaction is occurring in this process.

We can also notice from the reaction that is a reactant, and is a product. Therefore, the is being reduced to form . In order for this reduction reaction to happen, there needs to be a simultaneous oxidation reaction occurring, since the electrons need to come from somewhere. In this case, the electrons are coming from glucose-6-phosphate. Therefore, as is reduced to , glucose-6-phosphate is oxidized to ribulose-5-phosphate. Thus, this is an oxidation reaction.

Also, it's important to note that this is not a carboxylation reaction. In fact, it is actually a decarboxylation reaction, since one of the carbon atoms on glucose is converted into carbon dioxide.

Moreover, this is also not a phosphorylation reaction, as the reactant and products have an equal number of phosphate groups.

And lastly, this is not an isomerization reaction because glucose-6-phosphate and ribulose-5-phosphate have different molecular formulas, thus they cannot ever be structural isomers.

The pyruvate dehydrogenase complex catalyzes the following reaction:

Since it is product inhibited, acetyl-CoA will inhibit the complex.

From the question stem, we are shown the reaction in which glucose-6-phosphate is transformed into ribulose-5-phosphate. We are then asked to determine which type of reaction is occurring in this process.

We can also notice from the reaction that is a reactant, and is a product. Therefore, the is being reduced to form . In order for this reduction reaction to happen, there needs to be a simultaneous oxidation reaction occurring, since the electrons need to come from somewhere. In this case, the electrons are coming from glucose-6-phosphate. Therefore, as is reduced to , glucose-6-phosphate is oxidized to ribulose-5-phosphate. Thus, this is an oxidation reaction.

Also, it's important to note that this is not a carboxylation reaction. In fact, it is actually a decarboxylation reaction, since one of the carbon atoms on glucose is converted into carbon dioxide.

Moreover, this is also not a phosphorylation reaction, as the reactant and products have an equal number of phosphate groups.

And lastly, this is not an isomerization reaction because glucose-6-phosphate and ribulose-5-phosphate have different molecular formulas, thus they cannot ever be structural isomers.

Glycogen synthase is turned on when unphosphorylated. The enzyme responsible for this is protein phosphatase I. Protein kinase A inactivates glycogen synthase. Low glucose concentration causes a release in glucagon, which activates glycogen phosphorylase and deactivates glycogen synthase.