Glycolysis Enzymes | Some Important Points

Glycolysis Enzymes | Some Important Points

Glycolysis Enzymes

This article will discuss different Glycolysis Enzymes involved in glycolysis and the function of each one. We will also explore Pyruvate kinase, Glucose-6-phosphate, and Phosphofructokinase. It’s important to note that there are more than 100 different glycolysis enzymes, so we’ll discuss a few of them in this article. If you’re interested in learning more, please read the rest of this article!

Glycolysis Enzymes | Some Important Points


The phosphofructokinase glycolysis pathway is regulated by various factors, including the availability of high-energy phosphate (P), citrate, and Mg2+. The enzyme is a central component of the energy-producing process. Its rate-limiting activity is dependent on the availability of fructose 6-phosphate and citrate.

Both human and bacterial versions of the enzyme contain four subunits. The structure of the human enzyme is slightly larger and more complex. The active site is located in the middle of the beta-barrel. The enzyme removes one water molecule and replaces it with another during the reaction. The crystal structure shows how water is removed. There are two identical active sites within the enzyme. In the human enzyme, the magnesium ion anchors the phosphate molecule to the enzyme and holds it in its proper place.

Two phosphofructokinases are present in the human body. The first, phosphofructokinase-1, is involved in the catalysis of fructose-6-phosphate. PFK-1 catalyzes the first unique glycolysis step by converting fructose-6-phosphate to fructose-1,6-bisphosphate. The second phosphofructokinase enzyme, PFK-2, has phosphatase activity.

Phosphofructokinasein is another member of the glycolysis pathway. The enzyme transfers ATP to fructose-2-bisphosphate, and its activity is regulated by the allosteric effects of ATP and ADP. Increases in cytosolic ATP decrease PFK-1 activity. Consequently, glucose is shunted to storage.

Affected individuals have low or non-functional PFK levels. This can lead to hemolysis. PFK is essential for the phosphorylation of fructose-6-phosphate, the fuel of life. PFK is a key enzyme in the Embden-Meyerhof pathway. In some cases, PFK deficiency is a heterogeneous disorder. Infected individuals have a partial or complete loss of the PFK activity in muscle and erythrocytes. Affected individuals may also experience mild chronic hemolytic anemia.

Researchers have found PFK-1 isoenzyme patterns in breast cancer and para cancer tissues. The rate of glycolysis depends on the conversion of PFK-1 from PFK-L to PFK-P. This research acknowledges the work of Professor Changhua Wang and is supported by the eleventh Five-Year Key Programs for Science and Technology Development in China.

Pyruvate kinase

The pyruvate dehydrogenase complex catalyzes the oxidative decarboxylation of pyruvate, resulting in acetyl-CoA and CO2. The reaction is complete with the formation of CO2 and NADH. Despite this complex’s complexity, pyruvate kinase enzymes play an important role in glycolysis.

Several fatty acids, such as sterol, are produced by the enzyme. This process is regulated by insulin, which controls the fatty acid synthesis and b-oxidation. In addition, acetyltransferase is involved in the regulation of b-oxidation. Lastly, insulin regulates the production of acetyl-CoA carboxylase, a key enzyme in glycolysis.

How Do Enzymes Function?

Besides pyruvate kinase, other glycolysis enzymes include cholesterol esterase and pancreatic lipase. These enzymes hydrolyze fats and fatty acids in positions one to three and produce 2-monoacylglycerols. These products are stored in micelles, then transported to the bloodstream.

These enzymes can also activate adenylyl cyclase, a cell-derived protein, to initiate gene transcription. The MNEM alpha subunit inhibits adenylyl cyclase by binding to a ligand. Once activated, the enzyme cleaves PIP2 into IP3. Then, the enzyme phosphorylates the proteins in the cell.


In the body, glucose is metabolized into G6P by the enzymes hexokinase (PFK). Phosphofructokinase activity is tightly controlled and exerts a major influence on the rate of glycolysis. The enzyme is a tetrameric protein with two ATP binding sites. ATP lowers the enzyme’s affinity for fructose-6-phosphate. On the other hand, AMP increases the enzyme’s activity up to five times.

The enzymes cyclically involved in glycolysis work:

  1. Glycogen phosphorylase cleaves away glucose 1-phosphate from the glycogen chain.
  2. Phosphoglucomutase converts glucose 1-phosphate to G6P.
  3. Glucose 6-phosphatase cleaves off the phosphate group on G6P to release free glucose.

G6P is then transported through the bloodstream.

The cells adjust their metabolism according to the abundance of energy and nutrients. This ability to switch metabolism is essential to the growth of cells. Glucose-6-phosphate, the first intermediate in glucose metabolism, is a major component of the liver’s energy metabolism. The enzymes involved in the process function as a hub for metabolic pathways. It is also involved in hepatic glycolysis.

The production of glucose-6-phosphate glycolysis involves purification and kinetic assays. The primary biochemical pathways and enzymatic mechanisms are revealed through radiolabeling experiments. A detailed understanding of this process is necessary for its proper functioning. However, in the long run, enzymes can help prevent diseases. But what are the enzymes involved in glycolysis?

Glucose-6-phosphate dehydrogenase (G6PDH) is a widely distributed enzyme that catalyzes the first committing step of the pentose phosphate pathway. The oxidative PP pathway and the Entner-Doudoroff pathway are both fed by G6PDH. These enzymes affect the redox balance of the system and accept and reduce NAD+ similarly.

The liver is a crucial component in the regulation of blood glucose levels. It stores glucose after meals and produces it in the post-absorptive state. G6Pazases metabolize G6P in the liver, converted into glucose for storage. This glucose uptake and G6P release balance are vital for anteprandial glucose homeostasis.

Phosphoenolpyruvate kinase

Phosphoenolpyruvates are the main product of glycolysis, and several tissues express a corresponding isoform. There are three different isoforms of pyruvate kinase, PKM1, PKM2, and PKR. The PKM1 isoform is expressed by most adult tissues, while the PKM2 isoform is expressed only by the liver and kidney. PKR is found in red blood cells.

In glycolysis, phosphoenolpyruvate is the second source of ATP after adenosine. Phosphoenolpyruvate kinase catalyzes the transfer of the phosphate group from PEP to ADP, a practically irreversible and highly exergonic reaction.

Phosphoenolpyruvates are broken down into glucose and lactic acid. The enzymes can either degrade the glucose or the lactic acid. D-glucose can be degraded through a modified Entner-Doudoroff pathway, while D-galactose requires an Embden-Meyerhof-Parnas pathway.

However, phosphorylation of Bub3 by PKM2 may be an important checkpoint in mitosis. It may also signal cancer cells, which generate a higher demand for NADPH and produce more reactive oxygen species. Oncogenic signaling modulates the metabolism of proliferating cells, making it important to understand its role in cancer development.

Both PKM1 and PKM2 have an allosteric site for ATP. PKM2 accepts a wide range of protein substrates and has been found to use both ATP and PEP as phosphate donors. Despite the kinase’s role in glycolysis, it is important to note that these enzymes are related to the pyruvate phosphate dikinase.

The YPK protein contains four domains linked to the active site by a common parallel (a/b)8 barrel motif. The C-terminus contains the enzyme’s catalytic lysine, making it stable in the absence of NH4SO4.

In addition to PEP, the PKs have phosphoenolpyruvate carboxylase, which adds four-carbon-acetate to PEP. Malate is then transported to bundle sheath cells. Ultimately, PEP is converted into glucose, and gluconeogenesis occurs. The enzymes are responsible for the breakdown of carbohydrates into simple sugars.

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