Enzymes

Front 1

enzymes are

Back 1

biological catalysts and proteins

Front 2

enzymes have a

Back 2

specific shape due to chemical nature

Front 3

if enzymes lose their shape they

Back 3

can not function the way they are supposed to

Front 4

what do enzymes do

Back 4

lowers activation energy because surroundings does not have enough energy to get the two substrates to bond

Front 5

subtrates are essentially

Back 5

reactents

Front 6

enzymes shapes are specially designed for

Back 6

substrates to fit in

Front 7

lock and key theory

Back 7

substrate and enzyme have specific shape to fit together like a key fits in a lock, enzyme is lock, active sites are holes, substrates are the key

Front 8

active sites

Back 8

hole in enzyme where substrates fit in

Front 9

outside substances that can activate an enzyme are called

Back 9

co-factors and co-enzymes

Front 10

co-factors

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chemical metals that activate enzyme , exp magnesium, calcium, iron

Front 11

co-enzyme

Back 11

biological organic enzymes that activate the enzyme , exp protein

Front 12

once the enzyme is activated

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the enzyme and substrates combine, activation energy lowers and transition state occurs

Front 13

transition state

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Enzyme - Substrate Complex (E-S Complex)

Front 14

induced fit theory

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once everything is in place, the enzyme will change to a better fit, so that the substrates fit perfectly which encourages the bond to happen

Front 15

enzyme helping reaction occur is a

Back 15

anabolic reaction

Front 16

important key factors to reaction occuring

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shape specificity, induced fit theory

Front 17

factors that arent always neccasary for reaction

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co-enzyme and co-factors

Front 18

enzymes are

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reusable, catalysts

Front 19

why are enzymes reusable

Back 19

no chemical change so can be used over and over again

Front 20

inhibition

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when other molecules with similar shapes take substrates shape in enzyme which as a result deactivates enzyme

Front 21

competitive inhibition

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substance with exact or similar shape competes for the same active site to join enzyme

Front 22

non-competitive inhibtion

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substance not competing for same active site gets accidently placed in substrates active site and acts as a physical block or changes shape of enzyme so it can not function the same

Front 23

how many substrates can an active site hold

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1

Front 24

allosteric regulation

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a biochemical pathway where multiple enzymes do a smaller piece of a bigger job to create an endproduct like an assembly line

Front 25

what happens when too much end products produced

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energy is being wasted so once critical concentration is reached one extra end product will combine into starting enzyme to turn the enzyme off

Front 26

when you increase the enzyme

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rate increases until you hit a plateau where you have reached max substrate

Front 27

saturation point

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all enzyme and substrates reacting at same time

Front 28

when you increase substrate

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rate increases until all enzymes are used up then it plateaus

Front 29

when you increase temperature

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optimal temperature where enzyme perfroms the best, but after that point it damages enzyme. Will denature if in that temperature for a long time

Front 30

when you increase pH

Back 30

optimal pH where enzyme performs the best, but after and before that point can denature the bond