Lecture 3 Energy and Enzymes Flashcards

(31 cards)

1
Q

Forms of Energy

A
  1. Potential

2. Kinetic

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

Potential Energy

A

-Energy of position (stored Energy)

Ex.Chemical energy (in bonds)

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

kinetic Energy

A

-energy of motion

Ex. mechanicle Energy

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

Metabolism

A

-Sum of all chemical reactions in a living organism
include:
1.anabolism
2.catabolism

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

Anabolism

A
  • Biosynthesis reaction:building

- Endergonoc:require energy

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

Catabolism

A
  • Degradative reactions:Breaking down

- Exergonic:release energy

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

Chemical reactions

A
Components
-substrate:what goes in(reactant)
-product:what comes out
Directions 
-foward
-Reverse
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Factors affecting chemical reactions

A

1.law of mass action
2activation Energy
3.Enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Law of Mass Action

A
  • Foward Reactions
  • increase reactants you increase products
  • If you increase the product you will slow down production of the product
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Reversible Reactions

A

increase reactant or decrease product it will move to the right
Decrease reactant or increase product it will move to the left

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Activation Energy

A

-Minimum Energy required for reactants to overcome activation energy barrier to transition state tp product

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Enzymez

A

Structure:-protien based molecules
-substrate specific
Function:Reduce activation Energy
-Biological catalysts;

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

-Biological catalysts

A
  • speeds up reactions

- does not get used up or changed

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

Models for Enzyme binding

A
  1. lock and key mechanism

2. induced fit model

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

Lock and Key Mechanism

A
  • Substrate fit enzyme like a key to a lock

- problem:dosnt explain reversible reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Induced Fit model

A
  • substrate approximately fit enzyme

- After binding -> conformation change for better fit

17
Q

How Enzymes work

A

Enzymes bind with a substrate , converting the to products

18
Q

Enzyme Sites

A
  1. Active site:where substrate binds

2. Allosteric site:where other molecules (other than substrate) attch

19
Q

Types of Enzymes

A
  1. Simple Enzymes;protiens with catalytic activity

2. Holoenzymes:conjugated enzymes

20
Q

Holoenzyme Components

A

1.protien portion:Apoenzyme
2.Non-protien portion
-cofactor;inorganic ions
Ex.Iron,Zinc,Magnisum,Calcium
-coenzyme:Organic molecules(vitamine derivatiives)
Ex.NAD+, NADP+,FAD,coenzyme A

21
Q

Factors influencing Enzymatic rates

A
  1. Enzyme catalytic rate
  2. substrate concentration
  3. Enzyme concentration
  4. Affinity
  5. Temperatur
  6. pH
22
Q

Enzymes catalytic rate

A

Inherent speed of the enzyme

23
Q

Substrate concentration

A

increasing substrate, increases activity until saturation

24
Q

Saturation

A

Enzyme active site filled wit Substrate

25
Enzyme Concentration
Increase in enzyme= increase in maximum rate
26
Affinity
- How tightly a substrate binds to the active site | - High affening, increases reaction rates
27
Temperature
Enzymes have an Optimal temperature - increase rate of collision and reactions - to much heat will cause enzyme to denature(breaking of bonds)
28
pH
Enzymes have an Optimal ph | -Entreme pH will cause the Enzyme to denature
29
Enzyme Regulation
1. Allosteric Regulation | 2. Inhibitors
30
Allosteric Regulation
- modulater(weakly)bind to allosteric site 1. Activatior:increase catalytic rate - increase affinity to substrate 2. Inhibitor-Decrease Enzymatic Activity
31
Inhibitors
1.competitive;chemical that bind to active site Ex.Penicilin,sulfanilamide 2.Non-competitive:chemicals that bind to allosteric site or cofactors Ex.enzyme poisons(cyanine, Fluoride)