Enzymes

Front 1

shape of enzymes

Back 1

globular

Front 2

t/f: enzymes can speed up reaction by changing the equilibium constant

Back 2

f: enzymes cannot alter equilibrium constant

Front 3

Stage of reaction where old bonds break and new bonds form;

state with the highest energy

Back 3

transition state/ intemediate

Front 4

T/F: higher temp, higher rate of reaction

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F: at a certain temp, rate of rxn starts to slow down due to denaturation

Front 5

leads to the formation of the transition state species

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Ennzyme-Substrate complex

Front 6

bond between enzyme and substrate

Back 6

non-covalent

Front 7

Lock and key mechanism is AKA

Back 7

Fischer Mecchanism

Front 8

The Induced Fit model is aka

Back 8

Koshland Mechanism

Front 9

difference between Simple enzyme and Conjugated enzyme

Back 9

simple: protein only

conjugated: protein + nonprotein part

Front 10

the protein part of a conjugated enzyme

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apoenzyme

Front 11

the non-protein part of a conjugated enzyme

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cofactor

Front 12

biochemically active combination of apoenzyme and cofactor

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holoenzyme

Front 13

small organic factors can be found in ______

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vitamins

Front 14

inorganic cofactors can be found in _______

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minerals

Front 15

pertains to thee second number in systematic nain of enzymes

Back 15

the subclass

Front 16

peratins to the first number in systematicc naming of enzymes

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enzyme class

Front 17

pertains to the number of substrate molecules an enzyme can process per second

Back 17

turnover number/ catalytic rate constant

Front 18

an equation that describes how reaction velocity varies with substrate concentration

Back 18

Michaelis-Menten

Front 19

The michaelis menten equation

Back 19

Front 20

relationship of Km and Affinity

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inverse

Front 21

state where the formation of the ES complex is equal to the rate of breaking down of the ES complex

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steady state

Front 22

The double reciprocal plot for reaction velocity and substrate concentration

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lineweaver-burk plot

Front 23

equation for lineweaver-burk

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Front 24

shape of curve for allosteric enzymes

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sigmoidal

Front 25

shape of curve for non-allosteric enzymes

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hyperbolic

Front 26

a type of inhibition that creates a strong covalent bond with the enzyme

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irreversible

Front 27

a type of reversible inhibition that blocks substrate access

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competitive

Front 28

how to overcome a competitive inhibition

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by high substrate concentration

Front 29

measure of velocity at infinite [S]

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Vmax

Front 30

different site than substrate

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non-competitive

Front 31

measure of enzyme-substrate affinity

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Km

Front 32

a type of inhibition that does not affect enzyme substrate affinity

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non-competitive

Front 33

type of reversible inhibition that binds only to ES complex

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uncompetitive

Front 34

what happens to Km in an uncompetitive inhibition

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decreases; meaning better substrate affinity

Front 35

the six major classes of enzyme

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Oxidoreductase

transferase

hydrolase

lyase

isomerase

ligase

Front 36

Catalyzes oxidation reactions

Back 36

oxidase

Front 37

catalyzes reduction reactions

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reductase

Front 38

catalyzes forming a double bond by the removal of 2H

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Dehydrogenase

Front 39

Catalyzes transfer of amino group

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Transaminase

Front 40

Catalyzes transfer of phosphate group

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Kinase

Front 41

Catalyzes hydrolysis of ester bonds in lipids

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Lipase

Front 42

Catalyzes hydrolysis of amide bonds in proteins

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Protease

Front 43

Catalyzes hydrolysis of glycosidic bonds in carbohydrates

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Carbohydrase

Front 44

Catalyzes hydrolysis of sugar-phosphate ester bonds in nucleic acid

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Nuclease

Front 45

Catalyzes hydrolysis of phosphate ester bonds

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Phophatase

Front 46

A class of enzymes that catalyzes the reaction for the removal or addition of groups to form or beeak double bonds

Back 46

Lyasase

Front 47

Catalyzes reaction for the removal of H2O

Back 47

Dehydratase

Front 48

Catalyzes reaction for the removal of CO2

Back 48

Decarboxylase

Front 49

Catalyzes reaction for the removal of NH3

Back 49

Deaminase

Front 50

Catalyzes reaction for the addition of water

Back 50

Hydratase

Front 51

Catalyzes the reaction for flipping D to L isomers or vice versa

Back 51

Racemase

Front 52

Catalyzes the reaction for transfering functional groups within the molecule

Back 52

Mutase

Front 53

Catalyzes bond formation coupled by ATP

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Ligase

Front 54

Catalyzes reaction for the formation of new bonds between twwo substrates

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Synthetase

Front 55

Catalyzes reaction for the formation of new bonds between a substrate and CO2

Back 55

Carboxylase