Pyruvate kinase (PK) is an enzyme that is essential in the glycolysis process, which is the breakdown of glucose into pyruvate to produce energy in the form of ATP. PK is in charge of converting phosphoenolpyruvate (PEP) to pyruvate, a reaction that produces ATP via substrate-level phosphorylation.
PK can be found in all living organisms, from bacteria to humans, and is required for survival. PK is found in a variety of tissues in humans, including the liver, muscles, and brain. In mammals, there are four PK isozymes, each with tissue-specific expression patterns. PK is controlled by a number of mechanisms, including allosteric regulation, covalent modification, and gene expression.
Pyruvate kinase (PK) is an enzyme that is essential in the glycolysis process, which is the breakdown of glucose into pyruvate to produce energy in the form of ATP. PK is in charge of converting phosphoenolpyruvate (PEP) to pyruvate, a reaction that produces ATP via substrate-level phosphorylation.
PK can be found in all living organisms, from bacteria to humans, and is required for survival. PK is found in a variety of tissues in humans, including the liver, muscles, and brain. In mammals, there are four PK isozymes, each with tissue-specific expression patterns. PK is controlled by a number of mechanisms, including allosteric regulation, covalent modification, and gene expression. Allosteric regulation occurs when a molecule binds to a site on the enzyme other than the active site, causing a conformational change that alters the enzyme’s activity. A variety of metabolites, including ATP, ADP, and fructose-1,6-bisphosphate, regulate PK allosterically.
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