Enzyme activator

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Enzyme activators are molecules that bind to enzymes and increase their activity. They are the opposite of enzyme inhibitors. These molecules are often involved in the allosteric regulation of enzymes in the control of metabolism. An example of an enzyme activator working in this way is fructose 2,6-bisphosphate, which activates phosphofructokinase 1 and increases the rate of glycolysis in response to the hormone insulin.[1][2] In some cases, when a substrate binds to one catalytic subunit of an enzyme, this can trigger an increase in the substrate affinity as well as catalytic activity in the enzyme's other subunits, and thus the substrate acts as an activator.[3]

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  1. ^ Kurland IJ, Pilkis SJ (1995). "Covalent control of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: insights into autoregulation of a bifunctional enzyme". Protein Sci. 4 (6): 1023–37. PMC 2143155Freely accessible. PMID 7549867. doi:10.1002/pro.5560040601. Archived from the original on 2007-09-05. 
  2. ^ Okar DA, Lange AJ (1999). "Fructose-2,6-bisphosphate and control of carbohydrate metabolism in eukaryotes". BioFactors. 10 (1): 1–14. PMID 10475585. doi:10.1002/biof.5520100101. 
  3. ^ Voet, Donald; Voet, Judith; Pratt, Charlotte (2013). Fundamentals of Biochemistry: Life at the Molecular Level, Fourth Edition. John Wiley & Sons, Inc. p. 380. ISBN 1118129180.