2.4.3 the mechanism of enzyme action Flashcards

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1
Q

which 2 models explain the mechanism of enzyme action

A
  • lock & key hypothesis
  • induced fit hypothesis
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2
Q

why do the substrate molecules fit into the active site

A

due to the tertiary structure of the enzyme’s active site which gives it a shape complementary to the substrate molecule

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3
Q

which is the lock/key in the lock-and-key hypothesis

A

lock = enzyme’s active site
key = substrate//

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4
Q

describe the lock-and-key hypothesis to form smaller products

A
  1. substrate molecules are complementary to enzyme molecules active site
  2. substrates bind to active site & held by temporary hydrogen bonds = enzyme-substrate complex (ESC)
  3. substrate molecule is broken into smaller products which leave active site
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5
Q

describe the lock-and-key hypothesis to form a larger product

A
  1. substrate molecules bind to active site of enzyme molecule
  2. forms ESC & bonds form between substrate molecules
  3. larger product molecule leaves active site
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6
Q

what energy do the substrate/enzyme molecules have & what does this cause them to do

A
  • kinetic energy
    –> constantly moving randomly
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7
Q

what happens to the substrate molecules & what does this create

A
  • broken down/built up into product molecules = enzyme-product complex (still in active site)
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8
Q

what is the enzyme molecule now able to do

A

form another ESC

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9
Q

how many enzyme molecules are needed to convert a large number of substrate molecules into product molecules

A

small number

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10
Q

who modified the lock-and-key hypothesis (and when) - what did they suggest

A

1958 daniel koshland
–> suggested the enzyme isn’t a fixed/rigid structure but the presence of the substrate induces a shape change, providing a good fit

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11
Q

describe the induced fit hypothesis - refer to koshland/his suggestions

A
  • when the substrate fits into the enzyme’s active site, it changes SLIGHTLY to mould itself
  • moulding allows substrate to bind more effectively
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12
Q

what causes the active site to change shape

A

active site is complementary to the substrate BUT on binding, the subtle changes of the side chains (R-groups) of the amino acids (that make up active site) gives a more precise shape which exactly fits the substrate

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13
Q

which forces bind the substrate molecule to the enzymes active site once an ESC is formed

A

non-covalent forces eg. hydrogen bonds, ionic attractions, van der Waals forces & hydrophobic interactions

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14
Q

what’s formed when the products have been made but remain in the active site - induced fit hypothesis (still)

A

enzyme-product complex

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15
Q

what do enzymes lower

A

activation energy

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16
Q

what does heating chemicals during a reaction do & how

A
  • provide activation required for reaction
  • increases kinetic energy of molecules = move more (randomly) & more likely to successfully collide/react
17
Q

what would happen in the temp. was raised too high in a living cell

A

proteins within it would denature & lipids would melt

18
Q

how do enzymes reduce the activation energy for a reaction

A
  • bring specific substrate molecules close enough to react (without need for excessive heat)
  • thus, lower activation energy & speed up metabolic reactions