The pyruvate dehydrogenase complex essentially carries out a two part reaction: a decarboxylation and an oxidation. All these choices play important roles in the pyruvate dehydrogenase complex. Thiamine pyrophosphate (TPP) is the only choice, however, that is responsible for the decarboxylation step. Lipoamide acts as transporter, transferring the substrate to a distant active site. FAD then reoxidizes lipoamide for the next substrate. CoA is important in producing the substrate.

To see which of the enzymes in these answer choices may by in glycolysis, let's go through each one and look at their function.

Aldolase - This enzyme is indeed involved in glycolysis. It is responsible for the cleavage of fructose-1,6-bisphosphate into two products, glyceraldehyde-3-phosphate and dihydroxyacetone phosphate.

Thiolase - This enzyme catalyzes the the reversible association of two acetyl-CoA molecules into acetoacetyl-CoA. This is an important part of the mevalonate pathway as well as beta oxidation and ketone body synthesis/degradation.

Fructose-1,6-bisphosphatase - This enzyme is important in gluconeogenesis, a metabolic pathway that runs counter to glycolysis. Although many of the enzymes found in glycolysis are also used in gluconeogenesis, this enzyme is one example of an exception because it bypasses one of the irreversible reactions from glycolysis.

Aconitase - This enzyme is found in the citric acid cycle. Its function is to convert citrate into its isomer, isocitrate.

Hexokinase initiates the first step of glycolysis, which we know is the series of reactions by which glucose is processed to enter the citric acid cycle, and generate energy for the cell. So, in the case of glycolysis, glucose is the substrate of hexokinase. Based upon the name of the enzyme, we can infer that it phosphorylates a six-carbon molecule (which glucose is). By knowing the substrate is glucose, the correct product is glucose-6-phosphate, since its name indicates phosphorylation (addition of a phosphate group) to one of its carbons. Glycogen, fructose, and ATP are not involved in this first step of glycolysis. 

Hexokinase, pyruvate kinase, and PFK are regulatory enzymes in glycolysis, but PFK catalyzes the rate-limiting step (the phosphorylation of fructose-6-phosphate). Citrate synthase and isocitrate dehydrogenase are involved in the Krebs cycle, not glycolysis.

Glucokinase specifically phosphorylates the six-carbon sugar glucose. It is involved in glycolysis, but only in hepatocytes; hexokinase is the main enzyme that phosphorylates glucose during the first reaction of glycolysis. Rather, glucokinase's main role is to phosphorylate glucose to glucose-1-phosphate during the process of glycogen synthesis. The other kinases involved in glycolysis is phosphofructokinase. Fructose and mannose are not phosphorylated by glucokinase. Also, note that hexokinase has a higher affinity for glucose than does glucokinase.

Phosphofructokinase catalyzes the third step in glycolysis transforming fructose 6-phosphate to fructose-1,6-bisphosphate.  It is an irreversible step, and it is one of the major regulatory points of glycolysis.  One way in which it controls the flow of glycolysis is that when there is a high level of ATP, PFK is inhibited.  This is because the ultimate goal of glycolysis is to make ATP.  Thus, if there is already a high level of ATP, glycolysis should slow down.

Hexokinase catalyzes the first step of glycolysis, and this step requires the input of an ATP molecule. This step is unfavorable, but the steps catalyzed by the rest of the enzymes listed as answer choices are favorable.

In the fourth step of glycolysis, the six-carbon molecule fructose-1,6-bisphosphate is cleaved into two separate three-carbon molecules: dihydroxyacetone phosphate and glyceraldehyde-3-phosphate. This is catalyzed by the enzyme, aldolase.

Triose phosphate isomerase is responsible for converting dihydroxyacetone phosphate into glyceraldehyde-3-phosphate. It is glyceraldehyde-3-phosphate that continues on through glycolysis to ultimately form a pyruvate molecule. Therefore, if there is no triose phosphate isomerase, the dihydroxyacetone will be unable to continue through glycolysis. The normal net yield of 2 ATP will be halved, the production of NADH will be halved, and only 1 pyruvate molecule will be created. Glycolysis will still be able to function, and the energy investment phase will be unaffected.

Phosphofructokinase-2 converts fructose-6-phosphate to fructose-2,6-bisphosphate. The product, fructose-2,6-bisphosphate activates phosphofructokinase-1, the rate limiting step in glycolysis. Phosphofructokinase-2 is regulated by insulin (activated) and glucagon (inhibited).