enzymes Flashcards

1
Q

what is an enzyme

A

biological catalyst which speeds up a reaction

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2
Q

how do enzymes differ from chemical catalysts

A

higher reaction rates
act under milder conditions
greater specificity
can be regualtes

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3
Q

how are enzymes specicif

A

have aa in active site

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4
Q

properties of aa

A

different charges
different shapes
different pH

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5
Q

how does an enzyme bind to its substatea

A

substrate has to have the correct shape and charges in the right place to fit the active site
conformational change around the substrate

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6
Q

what is the transition state

A

highest energy point where bonds are strained

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7
Q

what do enzymes do to lower activation energy

A

stables the transition state complex
helps the bonds break in the transition states
(forms extra bonds)

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8
Q

why is there several peaks/troughs of activation energy

A

most reactions have several different transition states

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9
Q

Two main co factors

A

coenzymes

metal ions

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10
Q

what do coenzymes do

A

transfer chemical groups from one reactant to another

aid oxidation reduction reactions

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11
Q

what do metal ions do

A

coordinate negatively charged groups
i.e. prevents repulsion that would usually occur
accepte/donate e- in oxidation reduction reactions
provide charge and change shape

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12
Q

what is rate of enzyme reactions affected by

A

temperature
pH
substrate con

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13
Q

how does temperature affect rate

A

increase in vibrational energy of substrates

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14
Q

how does pH affect rate

A

causes different ionisation of functional groups leads to different charges in as

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15
Q

what does a low Km mean

A

high affinity

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16
Q

what dies a high Km mean

A

low affinity

17
Q

what is Km

A

how much substrate is required for the enzyme to work at half its maximal rate

18
Q

what is affinity

A

how well it binds to a substrate

19
Q

what is the Michaelis menten equation

A

Vi = Vmax{s}/Km + [s]

20
Q

what do statins compete with

A

HMG Co- reductase

21
Q

how are enzymes regulated

A

allosteric interactions
covelent modification
protein protein interaction
proteolytic cleavage

22
Q

how do allosteric interactions work

A

bind else where than AS which can alter the AS

23
Q

types of allosteric interactions

A

homotrophic

heterotrophic

24
Q

what is covalent moditifcation

A

regualte shape of AS

generally involved adding/removing phosphate

25
Q

what is protein protein interaction

A

interaction leads to AS shape change

26
Q

what are inactivate enzymes called once synthesized

A

zymogens

27
Q

what do enzymes cleave off an enzyme

A

prodomain

28
Q

what is it called when an enzyme chops iself

A

automatism