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Biology topic 1 (biological molecules) > enzymes > Flashcards

enzymes Flashcards

1
Q

whats a catalyst

A

a substance that speeds up a reaction without changing the substances produced or being changed itself

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2
Q

can catalysts be used again

A

yes

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3
Q

what are enzymes

A

biological catalysts that control the rate of reactions that take place in individual cells and in whole organisms

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4
Q

how are enzymes efficient

A

they dont change the conditions in cytoplasm when speeding up reactions
-remain unaffected and can be used again

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5
Q

what type of proteins are enzymes

A

globular proteins

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6
Q

how are enzymes produced

A

during protein synthesis as the mRNA transcribed from the DNA molecule us translated

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7
Q

why are enzymes so specific

A

as a result of their primary secondary tertiary and quaternary structure

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8
Q

specificity

A

features and functions of enzymes that means as a result of specific shapes each enzyme will only catalyse a specific reaction or group of reactions

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9
Q

what bonds hold proteins in enzymes together

A

intramolecular bonds

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10
Q

what effects the efficiacy of the enzymes

A

change in temp or PH

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11
Q

how do temp and PH effect efficacy of enzymes

A

they affect the intramolecular bonds within the protein that are responsible for the shape of the molecule

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12
Q

anabolic reactions

A

reactions that build new molecules inside cells

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13
Q

catabolic reactions

A

reactions that break down substances inside cells

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14
Q

metabolism

A

sum of anabolic and catabolic reactions in a cell

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15
Q

metabolic pathway

A

series of linked reactions in the metabolism of a cell

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16
Q

can enzymes slow down and stop reactions

A

yes

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17
Q

intracellular enzymes

A

enzymes that catalyse reactions within cells

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18
Q

extracellular enzymes

A

enzymes that catalyse reactions outside of the cell in which they were made

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19
Q

three types of names enzymes have

A

-short name of what enzyme works on or what it does with ase on end
-longer systematic name describing type of reaction being catalysed
-classification number

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20
Q

activation energy

A

energy reacting molecules need to have to break the chemical bonds that hold them together

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21
Q

how does raising the temp increase chemical reactions rate

A

by giving more molecules energy to react

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22
Q

why are enzymes needed to increase temp for reactions

A

normal cells couldnt survive under energy demand and extreme heat needed

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23
Q

how do enzymes cataylse reactions

A

by lowering the activation energy needed for the reaction to take place

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24
Q

what do enzymes have to do to lower the activation energy

A

form a complex with a substrate or substrates of the reaction

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25
Q

what happens once an enzyme reacts with a substrate

A

the products formed are released and the enzyme is free to catalyse more reactions

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26
Q

lock and key hypothesis

A

when active site has for for specific substrate

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27
Q

what lowers the activation energy

A

the formation of the enzyme substrate complex

28
Q

what happens when a complex is formed lock and key

A
29
Q

what happens once reaction complete enzymes lock and key

A

products no longer fit the active site and complex breaks up releasing products and freeing enzyme for more reactions

30
Q

induced fit hypothesis

A

active site more flexible and fits around substrate

31
Q

what happens once substrate enters active site induced fit

A

shape of site molded around substrate to form active complex

32
Q

what happens once reaction complete induced fit

A

enzyme reverts to inactive relaxed form waiting for another substrate

33
Q

how can you measure the way a factor effects the rate of reaction

A

the initial rate of reaction each time independent factor changed

34
Q

what must be kept in excess when measuring rate of reaction for enzymes

A

substrates unless substrate concentration rate is being measured

35
Q

whats the initial rate of reaction

A

when the reaction proceeds at its fastest rate

36
Q

whats the active site

A

a small depression in the enzyme caused by the way the enzyme is folded

37
Q

molecular activity

A

number of substrate molecules transformed by one enzyme per minute

38
Q

what happens when there are to many substrates

A

the enzymes become saturated and not enough enzymes so rate of reaction effected

39
Q

how does PH effect rate of reaction

A

PH effects R groups that hold together enzymes bonds

40
Q

how can some enzymes work at high temps

A

large amount of hydrogen and disulphide bonds

41
Q

enzyme inhibitors

A

stop enzymes from working

42
Q

reversible inhibitors

A

dont change enzyme forever

43
Q

2 types of reversible inhibitors

A

competitive and non competitive

44
Q

shape of competitive inhibitor

A

same shape as substrate

45
Q

what does competitive do

A

competes with substrate to form complex

46
Q

what happens if amount of inhibitor fixed

A

percentage of inhibition decreased by increasing substrate concentration

47
Q

what do non c do

A

form complex with enzyme or with enzyme substrate complex

48
Q

inhibition of non c

A

only effected by concentration of inhibitors not substrate

49
Q

how does inhibiton of non c work

A

change active site shape or complex of substrate and enzyme deform

50
Q

irreversible inhibitors

A

change enzyme forever

51
Q

inhibition of irreversible inhibitors

A

inhibitor combines with enzyme by permenant covalent bonding to one of the groups vital for catalysis to occur

52
Q

how do cells control so many reactions

A

-membrane compartment of reactions apart
-variations in PH can change rate of enzymes
-

53
Q

regulatory enzymes

A

have seperate site to active site where molecules can bond to have activating or inhibiting effect

54
Q

end product inhibiton

A

enzyme at begining of reaction inhibited by product at end

55
Q

describe the structure of starch

A

alpha glucose
glycosidic bonds
amylose has 1-4
amylopectin has 1-6 and 1-4
amylose is coiled
amylopectin branched
compact molecule

56
Q

explain what a catalyst is

A

speeds up rate of reaction
without being changed
lowers activation energy
provides different pathway

57
Q

whats hydrolysis

A

breaks glycosidic bonds
use of water

58
Q

why bread tastes sweet after chewing for long

A

maltose disaccharide
glucose mono
produced to taste sweet

59
Q

why is caffeine not an amino acid

A

no amine group
no carboxyl group
no R group

60
Q

why does malonate inhibit enzyme

A

it has similar structure so can bind into active site and act has competitive inhibitor

61
Q

why increasing temp of enzyme reaction changes rate of reaction

A

-higher Ek so more substrate enzyme complex formed
-high temps denature so less rate
-bond changes altering enzyme shape
-substrate no longer fits active site

62
Q

why rate of reaction decreases over time

A

hydrogen peroxide converted into products so less substrate to form complex with enzymes

63
Q

how tropolone effects rate at which grapes turn brown

A

tropolone similar to substrate
acts as competitive inhibitor
prevents from binding

64
Q
A
65
Q
A

Biology topic 1 (biological molecules) (11 decks)

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