Pyruvate Kinase
Pyruvate Kinase - Related Videos
01:15
Pyruvate Oxidation
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2019
After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells. First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
02:29
Pyruvate Assay for Estimation of Pyruvate Levels in Cellular Fractions of Worms
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2025
This video describes a colorimetric assay for quantitatively measuring pyruvate in the cellular fractions of Caenorhabditis elegans. Utilizing the hydrogen peroxide produced from the enzymatic reaction of pyruvate oxidase with cellular pyruvate, a chromogenic dye is oxidized to produce a colored product, measured using colorimetry to determine the pyruvate concentration.
01:20
Fates of Pyruvate
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2025
Pyruvate is the end product of glycolysis, where glucose is oxidized to pyruvate, simultaneously reducing NAD+ to NADH. Two molecules of ATP are also produced by substrate-level phosphorylation. In aerobic organisms, pyruvate is metabolized via the citric acid cycle to produce reduced coenzymes NADH and FADH2. These coenzymes are then oxidized in the electron transport chain to produce ATP and, in the process, regenerate the NAD+ and FAD. As seen in some cell types and organisms, fermentation...
02:54
Protein Kinases and Phosphatases
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2020
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven. Protein kinases Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
06:09
Assaying the Kinase Activity of LRRK2 in vitro
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Cited by 3 •
2012
Leucine Rich Repeat Kinase 2 is a large multidomain kinase, mutations in which are the most common genetic cause of Parkinson's disease. Analysis of the kinase activity of this protein has proven to be a crucial tool in understanding the biology and dysfunction of this protein. In this paper, in vitro assaying of the kinase activity of LRRK2 and a selection of its mutants is described, providing an experimental system to examine phosphorylation of putative substrates and potential dysfunction...
FAQs
During glycolysis, pyruvate kinase couples the high-energy phosphate transfer from phosphoenolpyruvate to ADP with ATP formation. This substrate-level phosphorylation directly supplies ATP. Because the reaction occurs at glycolysis’s endpoint, changes in enzyme activity can influence how much carbon proceeds toward pyruvate and how effectively glucose breakdown contributes to cellular energy production.
Pyruvate kinase responds to signals that reflect whether the cell has abundant fuel or energy. Fructose-1,6-bisphosphate can regulate the enzyme, while ATP and alanine provide additional metabolic signals. These inputs adjust glycolytic flux, meaning the rate through the pathway, so glucose breakdown can be coordinated with the cell’s broader metabolic state.
Comparing pyruvate kinase isoforms and mutation-associated changes helps researchers examine how variations in the enzyme relate to energy metabolism. This approach connects molecular differences with broader biological outcomes rather than treating glycolysis as a uniform process. The resulting context is especially relevant when investigating red blood cell function, inherited pyruvate kinase deficiency, or cancer biology.
Red blood cells are an important biological context for pyruvate kinase research because the enzyme’s metabolic role is relevant to their function. Investigating inherited pyruvate kinase deficiency therefore helps connect a molecular change with altered cellular energy handling. This relationship makes the enzyme useful for studying how glycolysis supports specialized cell functions.
In cancer biology, pyruvate kinase is examined as part of cellular metabolism. Its position in glycolysis makes its regulation relevant to how cancer cells manage carbohydrate breakdown and energy production. Research focused on this enzyme can place glycolytic behavior within the broader study of cancer metabolism while retaining attention to cellular energy status.
Potential metabolic therapies are one reason researchers study pyruvate kinase beyond basic pathway mapping. Information about its isoforms, regulatory signals, and mutations can frame questions about how changing enzyme activity might affect glycolytic flux. The enzyme therefore connects molecular regulation with inherited deficiency, red blood cell function, and cancer-related metabolic research.