Kinases vs Phosphatases & their roles in glycolysis and gluconeogenesis
Kinases transfer phosphoryl groups between organic molecules (often “adding” from ATP or similar). They’re classified as transferases. They can add or remove phosphoryl groups, but all is happening through transfer between organic molecules. Their directionality depends on relative “bond energies” & concentrations of the phosphate-containing molecules.
Phosphatases remove phosphoryl groups through hydrolysis (they use water to water to break a phosphoryl group off). They’re super unlikely to go in reverse (“add” phosphate group), so the reactions they catalyze are practically irreversible. They’re classified as hydrolases.
Many kinase reactions are also “irreversible” in vivo and these reactions are often key regulatory steps in pathways. Rather than regulating directionality by concentrations, cells often have a kinase and a phosphatase working as a pair and reciprocally regulated. This is often seen in signaling pathways, allowing kinases to be turned on and off in response to signals.
more on glycolysis & gluconeogenesis: blog: https://bit.ly/metabolicpathwayregula... ; YouTube: pt. 1 • Logic of glycolysis & gluconeogenesis... & pt. 2: • Metabolic pathway regulation logic - ...
more about all sorts of things: #365DaysOfScience All (with topics listed) 👉 http://bit.ly/2OllAB0 or search blog: http://thebumblingbiochemist.com
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