Chapter 4~ Enzymes Flashcards

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1
Q

what are enzymes

A

biological catalysts which speed up the rate of reaction without being used up itself by lowering the activation energy or by providing an alternative pathway

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2
Q

intracellular enzymes are
example

A

enzymes which act within cells
Catalase which ensures the breakdown of hydrogen peroxide into oxygen and water

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3
Q

extracellular enzymes are
example

A

work outside of cells which make them
amylayse and trypsin which are involved in digestion

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4
Q

what are the mechanisims of enzyme actions

A
  1. lock and key model
  2. the induced fit model
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5
Q

the lock and key model

A

the substrate fits into the enzymes active site the same way in which a key fits into a lock. the substrate shape and active site is perfectly complementary to eachother

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6
Q

lock and key model process1

A

1, substrate binds to active site forming an ENZYME SUBSTRATE COMPLEX
2. enzyme converts substrate into a product forming an ENZYME PRODUCT COMPLEX
3. product is released from enzymes active site

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7
Q

induced fit model

A

it suggests that the shape of the enzymes active site and substrate is not exactly complementary but when the substrate enters active site a conformational change occurs which induces catalysis

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8
Q

process of induced fit model1

A
  1. substrate enters enzymes active site forming an enzyme substrate complex
  2. enzyme undergoes a conformational Change causing substrate to change into product forming an ENZYME PRODUCT COMPLEX.
  3. product released into enzymes active site.
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9
Q

what are the factors affecting the rate of reaction

A

enzyme concentration, substrate concentration, temperature and PH

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10
Q

TEMPERATURE

A

as temperature increases, kinetic energy increases so particles move faster and colide this results in more sucessful frequent collisions allowing more ES complexes to form. however the enzyme becomes dentaured after optimum temperature as too much kinetic energy breaks the bonds between the amino acid r groups and so the shape of the active side changes and can no longer be complementary to the substrate decreasing the rate of reaction.

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11
Q

what is optimum temperature

A

the temperature at which the rate of activity pf enzymes is at its highest

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12
Q

what is the temperature coefficient

A

q10 it tells you how much a reaction rate changes when temperatures is raised by 10 degrees.

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13
Q

PH

A

Enzyme denatures above and below optimum PH.

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14
Q

enzyme concentration

A

enzyme conc increases, rate of reaction increases more active sites are availiable to bind to substrate this means more frequent collisions between enzyme and substrate so more ES COMPLEXES can form.

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15
Q

substrate concentration

A

substrate concentration increases, rate of reaction increases, more substrate molecules to fill enzymes active sites. more frequent collisions so more ES COMPLEXES

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16
Q

saturation point

A

all of the enzymes active sites are occupied with substrate molecules

17
Q

V max

A

maximum point of reaction.
all active sites are occupied by substrate particles so no more ES complexes can form

18
Q

cofactors

A

non protein molecules which need to be bound to an enzyme for it to work
it is also called a prosthetic group if bound tightly to enzyme with bonds.
inorganic
chemically unchanged

19
Q

coenzymes

A

organic molecules
chemically altered
they allow an enzyme to function and transfer chemical groups between enzymes

20
Q

enzymes are activated by ——
and inactivated by ——-

A

co factors
inhibitors

21
Q

competitive inhibitors

A

do not change v max
bind to active site of enzyme and block the substrate binding.

22
Q

non competitive inhibitor

A

bind to the site of an enzyme away from its active site known as the allosteric site.

23
Q

inactive percursor form

A

enzymes which can cause damage within cells producing them or to tissues where they are released or enzymes whose actions need to be controlled.
need to undergo change in shape to be activated done by adding a cofactor.

24
Q

end product inhibition

A

final product in a metabolic pathway which inhibits an enzyme that has acted earlier on in the pathway. it regulates metabolic pathways and controls amount of product produced.

25
Q

Djjejeje

A