Energy and Enzymes

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Last updated 3:17 PM on 6/12/26
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34 Terms

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exergonic reaction

energy moving outward

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endergonic reaction

energy moving inwards

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when the gibbs free energy is negative, it is a…

spontaneous reaction

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when the gibbs free energy is positive, it is a…

non spontaneous reaction

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spontaneous process definition

a process that can occur without energy input

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exergonic reaction example (in plants)

cell respiration

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example of endergonic reaction (in plants)

photosynthesis

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difference between endergonic reactions and exergonic reactions (spontaneity)

exergonic reactions are spontaneous, endergonic reactions are not spontaneous

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activation energy

the amount of energy needed for a reaction to take place

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effect that enzymes have on activation energy

they lower the activation energy barrier

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effects enzymes don’t have on reactions

they cannot change the free energy, they cannot make endergonic reactions exergonic

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the reactant an enzyme acts on:

substrate

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process of enzyme reaction in order

enzyme plus substrate, enzyme substrate complex, enzyme and product

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active site

region of the enzyme where the substrate binds to

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reason for enzyme specificity

complimentary fit between the shape of the active site and the shape of the substrate

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lock and key hypothesis

the substrate must fit in the active site in order to form the enzyme-substrate complex

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induced fit model

the substrate is not a perfect fit to the active site, so the enzyme slightly changes its shape when it bonds with the substrate

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2 weak chemical bonds that hold enzymes in the active site

ionic bonds and hydrogen bonds

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saturated enzyme

when all active sites of an enzyme are occupied by substrate molecules, enzyme is working at maximum capacity

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factors that affect enzyme functions

temperature and pH

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optimal conditions

conditions that favour the enzyme

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optimal temperature range for most enzymes

35 to 40 degrees celsius

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optical pH range for most enzymes

6 to 8

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effect of enzymes having the wrong pH/temperature

they become denatured, change shape and lose their function

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cofactors

nonprotein helpersfor chemical processes that cannot easily be carried out by the amino acids in proteins.

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example of chemical processes that cofactors are used for

electron transfers

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coenzyme

cofactor that is an organic molecule

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competitive inhibition

inhibitors that mimic the subtrate and compete with it for the active site

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solution to counteract competitive inhibitors

increase the concentration of substrates

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non competitive inhibition

inhibitor binds to another part of the enzyme, causing it to lose its shape and lessen effectivity

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pros of selective inhibition

controls cellular metabolism by regulating enzyme activity

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allosteric regulation

a regulatory molecule binds to a different site than that of the substrate, can cause inhibition or stimulation of the enzyme’s activity

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cooperativity

substrate molecule binds to site in multisubunit enzyme, triggers a change in all units, amplifies response of enzymes to substrates

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end product/feeback inhibition

an enzyme that catalyses one of a series of reactions is inhibited by the ultimate product of the pathway