enzymes Flashcards

(44 cards)

1
Q

enzyme

A

biological catalyst

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2
Q

birds and mammals

A

endotherms
maintain optimum body temp for enzymes
even if environment changes

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3
Q

catalase

A

breaks down hydrogen peroxide
(toxic molecules made in metabolic reactions)
2H20 –> 2H20 + O2

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4
Q

examples of living tissues with high amounts of catalase

A

liver cells
potato cells

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5
Q

what is a limiting factor? give examples

A

determines the rate of reaction when at a sub optimal level
eg temp
conc of substrate
conc of enzyme

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6
Q

bio washing powder

A

removes biological stains
contains enzymes
save energy/environment
can work at low temps
some only work at 40C

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7
Q

activation energy

A

minimum energy required to start a chemical reaction
enzymes lower activation energy by forming ESC
speeds up metabolic reaction without high temps needed

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8
Q

enzymes as a globular protein

A

tertiary structure
specific 3D shape
soluble in water
metabolic role

hydrophobic R groups inside
hydrophilic R groups inside

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9
Q

enzyme tertiary structure dependence

A

specific sequence of amino acids in a polypeptide chain
primary
secondary
R group interactions can alter 3D shape H+ OH-

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10
Q

intracellular enzymes

A

inside of cell
eg digestive enzymes inside lysosomes bacterium

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11
Q

extracellular enzymes

A

outside of cell
eg saliva (amylase starch–> maltose)

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12
Q

enzymes breaking down

A

catabolic
hydrolysis

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13
Q

enzymes building up

A

anabolic
condensation

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14
Q

renaturation

A

small pH changes away from optimum pH
back to optimum pH
active site returns to complementary

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15
Q

denaturation

A

big pH changes
cant return
active site will never fit again

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16
Q

how pH affects enzyme action

A

ACID pH below 7 -> high conc H+
ALKALI pH above 7 -> high conc OH-
changing these conc changes interactions of R groups and H bonds/ ionic bonds
changes active sire of R groups
tertiary structure of active site changes
substrate no longer binds
DENATURE

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17
Q

initial rate of reaction

A

rate of enzyme substrate reaction is highest when enzyme and substrate are initially mixed

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18
Q

low temps below optimum

A

less Ke
decreases collisions of substrate and active site PER SECOND
less ESC formed per second
slower rate of reaction

19
Q

high temp below optimum

A

more KE
more collisions of substrate and active site PER SECOND
more ESC per second
faster rate of reaction

20
Q

heat denaturing

A

temp increase molecules have more Ke
too much Ke so H bonds and ionic bonds break
active site 3D shapes changes
no longer complementary
no more ESC form

21
Q

optimum temp

A

highest rate of activity of enzymes
humans = 37C
thermophilic bacteria = 70C
cold climate organism = less than 5C

22
Q

inhibitor

A

substance that slow down the rate of reaction
affects the enzyme in some way

23
Q

competitive inhibitor

A

similar shape to substrate
can bind to active site
temporary reversible
prevents substrate binding to active site
effect can be reversed by increasing the conc of substrate

24
Q

examples of competitive inhibitors

A

STATIN
competitive inhibitor of enzyme used to synthesise cholesterol

ASPIRIN
irreversibly binds to active site of cox enzyme
prevents synthesis of prostaglandins and thromboxane
(produces pain and fever)

25
non competitive inhibitor
binds to allosteric site changes shape of active site increasing substrate has no effect on rate of reaction never reaches Vmax
26
examples of non competitive inhibitors
ORGANOPHOSPHATES irreversibly inhibit enzyme acetyl cholinesterase needed for impulse conduction leads to paralysis and death PROTON PUMP INHIBITOR used to treat long term digestion block enzyme that secrete H+ to the stomach
27
enzyme inhibitor as medicine
penicillin is an inhibitor of bacterial enzyme that help form cell wall of bacteria
28
cofactor
any substance that must be present for enzyme controlled reactions to take place at the appropriate rate
29
co enzymes as cofactors
organic small non protein usually vitamins bind loosely to active site co enzyme and charged take part in reaction they are then recycled also take chemical group from one enzyme to another forming a link
30
inorganic ions as cofactors
can bind with enzyme or substrate ion to enzymes can make ESC form more easily affects charge distribution/ shape of active site
31
prosthetic group
permanent part of enzyme contribute to final 3D shape of enzyme
32
affects enzyme controlled reactions
temperature pH conc of reactants presence of cofactors inhibitors
33
enzyme conc increases
initial rate increases when enzyme conc increases more active sites available more collisions more ESC formed more products ENZYME CONC IS LIMITING FACTOR some enzyme active sites are empty enzyme working working at Vmax increase in enzyme conc have no effect SUBSTRATE CONC HAS NO EFFECT
34
substrate conc increases
initial rate increases when substrate conc increases more collisions per second more ESC formed more products SUBSTRATE CONC IS LIMITING FACTOR all active site occupied enzymes work at Vmax an increase in substrate has no effect ENZYME BECOMES THE LIMITING FACTOR
35
measuring rate of reaction
METHOD 1 mass or volume/time = rate of reaction 1/time = rate of reaction
36
temperature coefficient Q10
measure of how much rate of reaction increases with a 10C increase Q10 = rate at 10C/ initial rate enzyme controlled reaction Q10=2
37
precursor activation 1
many enzymes formed in inactive form important for enzymes that could do damage to cells often need to undergo a change in 3D shape before cofactor added - apoenzyme after cofactor added - holoenzyme
38
precursor activation 2
sometimes achieved by action of another enzyme sometimes a changed in conditions such as pH/temp activates precursor by changing 3D structure these types of precursor called zymogens or pro enzymes
39
end product inhibition
used to control rate of reaction in cells ONLY WORKS WITH COMPETETIVE INHIBITORS final product inhibits the initial substrate further production of end product prevented in a process called end product inhibition of feedback inhibition
40
model
simple representation of a process understand how process works visual representations of a process
41
why is IDF is more accepted
x ray crystallography more closely fits induced fit model explains how enzymes lower the activation energy puts stress on molecules in substrate less energy to break
42
lock and key model
active site is fully formed + rigid fully complementary to substrate doesnt explain the reduction of activation energy doesnt explain changing shape of enzyme
43
pellagra
disease caused by lack of vitamin B3 causes inflamed skin dementia diarrhoea sore in mouth
44
induced fit model
active site is not fully complementary to the shape of the substrate active site has charged amino acids opposite to those of the substrate substrate randomly collides with active site enzyme changes shape active site becomes complementary to the substrate forms an enzyme-substrate complex active site fits more closely around substrate charges holds substrate in place change in enzyme active site puts strain on substrate destabilises bonds in substrate lowering activation energy produces enzyme product complex products formed are a different shape to substrate no longer complementary to the active site and leave it