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
what is protein protein interaction
interaction leads to AS shape change
26
what are inactivate enzymes called once synthesized
zymogens
27
what do enzymes cleave off an enzyme
prodomain
28
what is it called when an enzyme chops iself
automatism