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| is the capacity to do work, or the capacity for change |
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| is stored energy- as chemical bonds, concentration gradient, charge imbalence |
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| sum total of all chemical reactions in an organism |
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complex molecules are made from simple molecules
-energy is required = endergonic |
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complex molecules are broken down to simpler ones
-energy is released = exergonic |
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| T or F anabolic and catabolic reactions are usually linked |
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apply to all matter and all energy transformations in the universe
-help us understand harvest and transformation of energy to sustain life |
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| First Law of Thermodynamics |
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Energy is neither created nor destroyed
- total energy before and after conversion is the same |
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| Second Law of Thermodynamics |
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| when energy is converted from one form to another some of that energy becomes unavailable to work |
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| T or F energy transformation is 100% efficient |
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| is a measure of the disorder in a system |
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| T or F It takes energy to impose order on a system |
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| Total energy/ enthalpy (H) = |
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| free energy(G) +entropy(S) * T(absolute temperature) |
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| changes in free energy can be measured in |
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| Magnitude of change in G depends on |
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-change in total energy
-change in entropy- large changes = G becomes (-) |
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| T or F If free energy is not available the reaction still occurs |
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| hydrolysis of a protein into its components of amino acids is an example of |
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| T or F Disorder tends to increase because of energy transformations( 2nd Law of Thermodynamics) |
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| T or F living organisms must have a constant supply of energy to maintain order |
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reactions release free energy (- change in G) = disorder
-complex to free energy and small molecules |
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consume free energy(+ change G) = order increases
-free energy and small molecules to complex |
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forward and reverse reactions occur at the same rate
-change in G = 0 |
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| T or F values near zero change in G are characteristic of readily reversible reactions |
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| T or F a lower concentration of A or B will favor the reaction moving in one direction |
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| False - higher concentration |
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| T or F change in G is related to the equilibrium point |
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True
-more (-) change in G = further from completion and more free energy is released |
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is a nucleotide that captures and transfers free energy
-releases large amount of energy when hydrolyzed
-can phosphorylate or donate phosphate |
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-exergonic
-ATP + H20 = ADP + Pi+free energy |
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-endergonic
ADP + Pi+free energy = ATP + H20 |
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| T or F formation and hydrolysis of ATp separate exergonic and endergonic reactions |
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| Examples of Exergonic Reactions |
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-cell respiration
-catabolism |
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| Examples of Endergonic Reactions |
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-active transport
-cell movement
-anabolism |
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| T or F most biochemical reactions require a catalyst to allow the reaction to occur efficiently |
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-biological catalyst
-speed up the rate of reaction
-not altered by reaction |
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| the amount of energy required to start the reaction |
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| Transition State Intermediates |
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| energy changes the reactants into unstable forms with higher free energy |
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| T or F activation energy can come from heating the system |
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| T or F enzymes lower the energy barrier by bringing the reactants together |
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| T or F Enzymes are not highly specific and is not determined by their 3-D shape |
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| bind to the active site of the enzyme forming an enzyme -substrate complex |
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Enzyme-Substrate Complex(ES)
E+S = ES = E+P |
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| is held together by hydrogen bonds, electrical attraction, or covalent bonds |
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| T or F the enzyme may change when bound to the substrate but returns to its original form |
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| T or F when enzymes lower the energy barrier the final equilibrium and change in G change |
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| Different ways enzymes work |
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-in catalyzing reaction- it can use one or more mechanisms
-orient substrate molecules
-can stretch the bond in substrate molecules making them unstable
-can temporarily + chemical groups to substrates |
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| Shape of enzyme active site allows a specific substrate to fit called |
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| Binding of a substrate to an enzyme active site |
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-depends on hydrogen bonds
-electrically charged groups
-hydrophobic interactions |
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| enzymes change shape when they bind to the substrate |
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| non-amino acid groups bound to enzymes |
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| small carbon-containing molecules, not bound permanently to enzymes |
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| T or F the rate of a catalyzed reaction depends on substrate concentration |
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| T or F the concentration of an enzyme is usually much higher then concentration of a substrate |
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| all enzyme is bound to substrate = maximum rate of reaction |
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| is used to calculate enzyme efficiency= molecules of substrate converted to product per unit time |
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-each reaction is catalyzed by a specific enzyme
-pathway is interconnected
-occur simultaneously |
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| T or F regulation of enzymes and reactions rates do not help maintain internal homeostasis |
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regulate enzymes by binding to the enzyme or slow reaction rates and regulate metabolism
-stabilize an inactive form of the enzyme = can't bind to substrate |
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inhibitor covalently bonds to the side chains in the active site - permanently inactivates the enzyme
ex: DIPF or nerve gas |
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| inhibitor bonds non-covalently to the active site and prevents substrates from binding |
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compete with the natural substrates for binding sites
-when concentration of competitive inhibitor is reduced = detaches from active site |
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| Noncompetitive inhibitors |
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bind to the enzyme at a different site
-enzyme changes shape and alters the active site |
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-ex: competitive inhibition
an effector molecule binds to an enzyme's regulatory subunit = enzyme changes shape
-important in regulating metabolism
-have a sigmoid shape |
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effectors that stabilize an active enzyme
-can bind to substrate |
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| T or F most allosteric enzymes are proteins with quaternary structure |
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| Commitment Step in metabolic pathways |
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| the final product acts as a noncompetitive inhibitor of the first enzyme, which shuts down the pathway |
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| T or F ph influences the ionization of functional groups |
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| at high temperatures, non-covalent bonds begin to break in the enzyme |
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| enzymes that catalyze the same reaction but have different optimal temperatures |
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| T or F humans have lover optimal temperature than enzymes in most bacteria |
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