Enzymes Flashcards

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1
Q

What do anabolic reactions do

A

build up molecules e.g protein synthesis

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2
Q

What do catabolic reactions do

A

break down molecules e.g digestion

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3
Q

What are enzymes

A

globular proteins that act as catalysts

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4
Q

Why are enzymes called biological catalysts

A

Because they are made of living cells

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5
Q

What is the structure of an enzyme

A

Protein with tertiary structure
Hydrophillic R groups on the surface making it soluble
Particular sequence of amino acids
R groups determine shape and bonds that form

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6
Q

What is the active site

A

specific 3D site which substrate binds to by weak chemical bonds

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7
Q

what are the general characteristics of enzymes

A

speed up reactions
not used up
have a high turn over rate
only catalyse reactions that are energetically favourable

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8
Q

what are the 3 sites of enzyme action

A

extracellular
intracellular in solution
intracellular membrane bound

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9
Q

what is an example of an enzyme acting extracellular

A

enzymes secreted from cells in exocytosis

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10
Q

what is an example of an enzyme acting intracellular in a solution

A

in solution inside cells e.g glucose breakdown in glycolysis

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11
Q

what is an example of an enzyme acting intracellular membrane bound

A

attached to membranes e.g mitochondria in ATP formation

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12
Q

what is the lock and key model

A

the active site and substrate are complementary to each other and it is a specific fit

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13
Q

what is the lock and key model

A

the active site shape changes slightly to acomodate the substrate

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14
Q

how do enzymes speed up the rate of reaction

A

they modify the substrate so that the reaction requires a lower activation energy
when substrate enters active site the molecules alters the shape so reactions can occur at lower temp

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15
Q

what is activation energy

A

minimum energy required in a chemical system for a reaction to occur

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16
Q

what is the first limiting factor in a reaction

A

the enzyme conc

17
Q

what is the limiting factor as the reaction carries on

A

the substrate conc

18
Q

how do you calculate rate of production

A

increase in mass divided by time

19
Q

how do you calculate % increase in mass

A

actual increase in mass divided by initial mass X100

20
Q

what is inactivation

A

reversible reduction of enzyme activity at low temp
insufficient energy to form E+S complexes

21
Q

what happens to enzymes over 40 degrees

A

denature due to increasing breaking hydrogen bonds and altering the enzymes tertiary structure

22
Q

what happens to enzymes at low temps

A

they become inactivated

23
Q

what happens to enzymes if PH is too high

A

it becomes neutralised by positive OH- charges

24
Q

what happens to enzymes if the PH is too low

A

the H+ ion attracts negative charges and neutralises them

25
Q

What is enzyme inhibition

A

the decrease in the rate of an enzyme controlled reaction by an inhibitor

26
Q

What does an inhibitor do

A

binds with the enzyme and stops it from forming an enzyme substrate complex

27
Q

What is the effect of substrate concentration on enzyme activities

A

the more substrate the more successful collisions and complexes formed

28
Q

What is the effect of enzyme concentration on activity

A

as enzyme concentration increases there are more active sites available so more complexes can form

29
Q

What is the effect of pH on enzyme activities

A

too High
Neutralised by excess OH-ions
Too low
The H+ions neutralise negative charges
Both of these disrupt ionic and hydrogen bonds which changes the shape of the active site

30
Q

How are enzymes immobilised

A

fixed trapped or bound on an inert matrix

31
Q

What materials can be used to immobilise an enzyme

A

sodium alginate beads or cellulose microfibrils

32
Q

How do immobilised enzymes work at higher temperatures and pH

A

It creates a microenvironment because trapping the molecule prevents the shape change that would denature the active site

33
Q

what is an example of an inhibitor being used and how does it work

A

lactose free milk
milk passed through a column with immobilised lactase
lactose binds to active site and is broken Down

34
Q

what are the advantages of immobilised enzymes

A

increased stability and function over a wide range of temperatures and pH
products not contaminated
enzymes easily recovered for reuse

35
Q

why do enzymes trapped in beads have lower rate of reactions

A

because as is inside bead so substrate has to diffuse
readily available to bind on a matrix

36
Q
A