Aldolase is defined as a member of the principal glycolytic enzyme family. These enzymes are responsible for catalyzing the conversion of d-fructose-1, 6-diphosphate into dihydroxyacetone phosphate and d-glyceraldehyde-3-phosphate. It does this through the glycolysis metabolic pathway.
This enzyme is most likely found in all cells. But,more significant concentrations are commonly found in muscle, brain, and liver tissues. People with increased levels of aldolase were found to have a myotonic muscle disease.
Aldolase is found in the cytoplasm and nucleus of cells. As of right now, there are a total of three aldolase isoenzymes discovered. These are referred to as Aldolase A, B, and C. Type A is considered a muscular type and is regularly found connected to the cytoskeleton.
This gene contains 8 exons and the 5' UTR ID. A variety of crucial amino acids have been identified that are held responsible for its catalytic function.
Aldolase Mechanism & Interactions
There are two key amino acids involved in the reaction caused by aldolase. These are lysine and tyrosine. Lysine helps covalently bind and stabilize the intermediates. On the other hand, the tyrosine acts as a very efficient hydrogen acceptor.
As mentioned earlier, aldolase binds to the cytoskeleton. It does this by attaching to the containing filament that's on the cytoskeleton. By connecting to these filaments, it lets the enzyme regulate cell contractions.
Aldolase is regulated by a handful of energy metabolism substrates. These include glucose, lactate and glutamine. When human mast cells are looked at, this enzyme is seen to behave differently. It goes through a post-translational regulation by protein tyrosine nitration. As such, this can alter its affinity for FBP and IP3. Consequently, this alteration affects IP3 and PLC signaling cascades.
This enzyme plays a pivotal role during the fourth step of glycolysis. In layman's terms, it helps convert sugar into energy through all the cells in the body. Not only that, but it also plays a role in the reverse pathway; gluconeogenesis. As stated earlier, it catalyzes the conversion of d-fructose-1, 6-diphosphate into dihydroxyacetone phosphate and d-glyceraldehyde-3-phosphate. It does this by the aldol cleavage of the C3-C4 bond.
Consequently, it's also one of the key players in ATP biosynthesis. There have also been strong links that connect the function of aldolase to other muscle functions as well. This includes muscle maintenance, along with striated muscle contractions. Some studies also present findings that show it helps with cell shape regulation and motility, actin cytoskeleton organization and cell proliferation regulation. Due to the function, aldolase is expressed in most tissues. However, it's commonly seen during the development of the embryo and adult muscle. When muscle damage occurs, aldolase levels in the blood are seen to rise. As such, a blood test used to figure out aldolase levels is commonly used to help diagnose certain diseases/conditions affecting the skeletal muscle. This enzyme is also highly expressed in different cancers. Many researchers indicate that too much aldolase enhances glycolysis in these cancer cells. As such, it leads to rapid growth. Thus, the downregulation of this enzyme is seen to reduce cell motility and tumorigenesis. As a result, aldolase is seen as a possible therapeutic drug target.