Which one of the following statements about the control of enzyme activity by i Phosphorylation of an enzyme results in a conformational change Phosphorylation of an enzyme occurs only at specific tyrosine residues Phosphorylation of an enzyme is carried out by phosphoprotein phosphatases Enzyme control by phosphorylation is irreversible
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Given the four statements, which is the correct statement about the control of enzyme activity by phosphorylation
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- The capacity to do work best defines: a metabolic pathway. entropy. kinetic or potential energy. a chemical equilibrium. thermodynamics.Glycogen phosphorylase, an enzyme that catalyzes the breakdown of glycogen to form glucose, is active when a phosphate group is added. This is an example of enzyme regulation by ____________________________.Which of the following correctly describes the relationship between an enzyme and its function Glycogen phosphorylase: synthesis of glycogen Phosphate: removal of a phosphate group Adenylyl cyclase: conversion of cAMP to AMP Kinase: addition of a lyrosine
- Why is glucose phosphorylated to become glucose-6-phosphate? Group of answer choices to isomerize it to glucose 1 phosphate to activate the enzyme hexokinase to trap glucose inside the cell and commit it to the pathway to form bisphosphate moleculesThe three irriversible reactions in glycosis is : Hexoknase, PFK-1 and Pryvate kinases. they are all enzymes, why these three enzymes are irriversible? the explaination below is not very understandble. "Hexokinase: This enzyme catalyzes the conversion of glucose to glucose-6-phosphate. This reaction consumes ATP and traps glucose inside the cell by converting it into a charged and phosphorylated form. Phosphofructokinase-1 (PFK-1): This enzyme catalyzes the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate. This reaction is the committed step of glycolysis, and it is also the main regulatory point of the pathway. PFK-1 is allosterically inhibited by ATP and citrate and activated by AMP and fructose-2,6-bisphosphate. Pyruvate kinase: This enzyme catalyzes the conversion of phosphoenolpyruvate (PEP) to pyruvate, producing ATP. This reaction is the last step of glycolysis and is also highly regulated. Pyruvate kinase is allosterically activated by fructose-1,6-bisphosphate…Which of the following is NOT true about enzymes? Enzyme inhibitors interact reversibly or irreversibly with an enzyme to alter its Km and /or Vmax values. Enzymes typically act under milder conditions of temperature and pH than non-enzyme chemical catalysts. Zymogens are the inactive precursors of enzyme. Nucleophilic groups can catalyze reactions through the transient formation of covalent bonds with the substrate. Transition state stabilization can significantly increase the activation energy for a reaction.
- Several of the enzymes of glycolysis fall into classes that we will see often in metabolism. What reaction types are catalyzed by each of the following: Kinases Isomerases Aldolases DehydrogenasesThe Effect of Various Factors on the Rate of an Enzyme Reaction. These experiments will use the enzyme catalase, which is found in potatoes. Catalase acts on the substrate, H2O2 (hydrogen peroxide), to produce H2O and O2. The O2 is released as bubbles. Therefore, the more bubbles you see, the greater the reaction. Base your responses on the following data table: The effect of temperature on the rate of enzyme reactions Tube Pre-Treatment Temp °C Treatment Temp °C Prediction - no bubbles + some bubbling ++ strong bubbling +++ very strong bubbling Observations - no bubbles + some bubbling ++ strong bubbling +++ very strong bubbling C1 100 100 +++ - C2 25 25 ++ +++ C3 0 4 + ++ What do you conclude about the effect of temperature on enzyme activity? Don’t just say that it has an effect, say how it affects it. Based on your conclusion, do you think you might digest ice cream at a slower or faster rate than a hot soup?The enzyme catalase is found in beef liver. This enzyme is responsible for the rapid breakdown of hydrogen peroxide to water and oxygen. When the catalase in the liver works properly, the speedy release of O2 and H2O will cause a foaming effect. When the enzyme activity increases, there is more foaming, and when the enzyme activity decreases, there is less foaming. If the enzyme becomes denatured, there will be no foaming.
- Enzymatic reactions within a cell are often specific for their substrates. Enzymes that use ATP will not efficiently use dATP. Enzymes that use NADH cannot use NADPH instead and enzymes that work on alpha glucose can’t work on beta glucose linkages. What physical property of enzymes causes them to be so picky?Which is the most versatile (related to bonding) glycogen metabolism (catabolism or anabolism) enzyme? What bond(s) does this enzyme make and/or break? Enzyme: Make: Break:What type of enzyme is responsible for initiating the process of glycolysis? Hydrolase. Dehydrogenase. Kinase. Phosphatase. Phosphorylase.