Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

as biology module 2 > 2.4 Enzymes > Flashcards

2.4 Enzymes Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

Enzymes

A
  • Globular proteins
  • Catalysts
  • Specific
  • active site
  • pH
  • Temperature
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Catalysts

A

-Speed up the rate of reaction without being used up

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Specific enzymes

A

-only work one molecule called a substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

substrate

A
  • the substance that the enzyme interacts with

- complementary shape to an enzyme’s active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

active site

A

the part of the enzyme that the substrate molecules bind to

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

how do enzyme carry out reactions?

A

enzymes lower activation energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

activation energy

A

the amount of energy needed to start a reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

activation energy and rate of reaction

A
  • the lower the activation energy
  • the less energy needed
  • so the reaction happens quicker
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what happens in an enzyme reaction?

A
  • substrate binds to active site
  • Enzyme will break the bond and split it into two little products
  • 2 products form joined together
  • new bigger products form
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Lock and Key Model

A

substrate has an exact right shape, it fits into active site
- like a key fits into a lock

  • stays there until it is broken apart or joined together
  • complementary shape
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Induced Fit Model

A
  • the shape of the enzyme is slightly different to the shape of the substrate
  • the active site will be complementary to the substrate but the whole enzyme structure will be different
  • substrate will push its way in and the enzyme will close around it creating more tight fit to prevent breaking away
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Factors affecting enzyme activity and rate of reaction

A
  • Temperature

- pH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Temperature and enzyme activity

A

-More kinetic energy
-More collisions
-Enzyme vibrates
Weak bonds broken
-Loses shape
-Denatures

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

what is pH

A

measure of H+ ions
above 7 = OH- ions
below 7 = H+ ions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

pH and enzyme activity

A
  • More H+ or OH-
  • Interfere with bonds
  • loses shape
  • Active site loses shape
  • Denatures
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Enzyme Concentration and Rate of Reaction

A
  • More enzymes
  • more active sites
  • More collisions
  • more enzyme-substrate complex formed
  • rate of reaction increases to a point
  • more enzyme, no more substrates to bind with
  • rate of reaction will stay the same

-substrate concentration a limiting factor

17
Q

Substrate Concentration and rate of reaction

A
  • More substrates
  • faster reaction
  • more collisions
  • more active sites used
  • rate of reaction increases to a point

-enzyme concentration a limiting factor

18
Q

Inhibitors

A
  • Reduce the rate of reaction
  • Bind to enzymes
  • Competitive
  • Non-competitive
19
Q

Competitive inhibitors

A
  • binds to enzyme
  • substrate can no longer bind with enzyme
  • can’t react as it isn’t complementary but still fits into enzyme
  • rate of reaction is decreased
20
Q

Non-competitive inhibitors

A
  • binding to enzyme away from active site
  • changes active site shape so substrate can no longer fit in
  • enzyme substrate complex cannot form
  • rate of reaction decreases
21
Q

Cofactors

A

-non-protein substances bound to enzymes

Cofactors must be present in some enzymes

22
Q

Types of cofactors

A
  • Coenzymes
  • Prosthetic groups
  • inorganic ion cofactor
23
Q

Coenzymes

A
  • Small, organic, non-protein molecules
  • Changed and used in the reaction
  • Recycled
24
Q

Prosthetic groups

A
  • permanent part of the molecule
  • Usually transmission metal
  • Contribute to 3D structure
25
Q

inorganic ion cofactor

A
  • increases rate of reaction

- Makes it easier for enzyme-substrate complexes to form

26
Q

How a competitive inhibitor works?

A
  • Complimentary shape
  • Binds to active site
  • Limited time
  • Prevents enzyme substrate complex
  • Less product
27
Q

How an increase of substrate molecule effects rate of reaction?

A
  • Rate increased
  • Greater chance of substrate binding with active site
  • More product
  • Will reach maximum rate of reaction

as biology module 2 (13 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions