Energy released from the downhill reactions of catabolic pathways can be stored and then used to drive the uphill reactions of the anabolic pathways.
Kinetic energy is energy associated with relative motion of objects. An object not presently moving may still possess energy, potential energy
Free energy is the proportion of a system”s energy that can perform work when temperature and pressure and uniform throughout the system, a living cell. G=free energy= H- T(S). H- the system enthalpy or total energy. S= change in the system”s entropy. T= temperature in kelvin. G is negative when either H is negative or T(S) is positive or both. Also G= G final state- G initial state
Negative Exergonic reactions proceeds with a net release of free energy. G is negative because it loses free energy. Greater decrease in free energy, greater amount of work done
Is cellular respiration an endergonic or an exergonic reaction? What is the delta G for the reactions?
Endergonic reactions absorb free energy. G is positive because it stores free energy in molecules. A cell that has reached metabolic equilibrium is dead. Cellular respiration is exergonic. G is negative
Endergonic. Plants get required energy from the environment by capturing light and converting its energy to chemical energy. Next is a series of exergonic steps that use energy to make glucose molecules.
Chemical work: pushing of endergonic reactions that would not occur spontaneously, such as synthesis of polymers from polymers to monomers. Transport work: Pumping of substances across membranes against the direction of spontaneous movement. Mechanical work: contraction of muscle cells.
When the terminal phosphate bond is broken, a molecule of inorganic phosphate is formed, and energy is ______
In many cellular reactions, a phosphate group is transferred from ATP to some other molecule in order to make the second molecule less stable. The second molecule is said to be _______
Activation energy is the amount of energy needed to push the reactants to the top of an energy barrier, or uphill, so that the downhill part of the reaction can begin.
Without affecting the free energy change (G) for a reaction, an enzyme speeds the reaction by reducing its activation energy
Reactant an enzyme acts on. The enzyme binds to its substrates forming an enzyme substrate complex. This leads to the enzyme converting substrates to the products of the reaction.
Typically a pocket or groove on the surface of the enzyme where catlysis occurs. Area where enzyme binds to substrate.
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Brings chemical groups of the active site into positions that enhance their ability to catalyze the chemical reaction. Shape change makes the active site fit even more snugly around the substrate.
Enzymes are usually very specific as to which reactions they catalyze and the substrates that are involved in these reactions. Complementary shape, charge and hydrophobic characteristics of enzymes and substrates are responsible for this specificity.
Act as a template for substrate orientation. Stabilize transition states, stressing substrates ,provide favorable microenvironment, or participate directly in catylic reactions
The more substrate molecules that are available, the more frequently they access the active sites of the enzyme molecules.
Optimal pH values for most enzymes fall in the range of pH 6-8. Just like temperature, there is an optimal range where the enzymatic reaction increases.
Rate of enzymatic reaction increases with increasing temperature, partly because substrates collide with active sites more frequently when the molecules move rapidly. However if it gets too high, speed of the enzymatic reaction drops sharply and denatures.
Cofactors are nonprotein helpers for catylic activities. Coenzymes are organic cofactors. Coenzymes are vitamins, cofactors are things like zinc and iron.
They both inhibit the enzyme from doing its job. Competative inhibitors compete with substrates to attach to active site. Noncompetitive inhibitors do not compete and just attach to a different area.
Neither bind directly to the active site. In allosteric though, it does not only work on one subuniti, it works on many.
The activator stabilizes the shape with the final active site. The inhibitor stabilizes inactive form of the enzyme.
Hemoglobin has a higher affinity for O2 when there is more O2, so in places like the lungs, it gets more O2, wile in places where there is less, it”s affinity for O2 will drop.
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