Enzymes - Organic Catalysts (carbon & hydrogen) Flashcards

You may prefer our related Brainscape-certified flashcards:
0
Q

Structure of Enzymes

-cofactors

A

Enzymes are proteins
Enzymes that require additional non-protein parts are called:
COFACTORS- additional chemical components of an enzyme (not proteins)–(minerals & vitamins - help out enzymes)
(Eg. Iron, calcium, copper & zinc)
If the cofactor is an organic molecule its is called a COENZYME

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

Catalysts

A
  • Molecules that speed up (catalyze) chemical reactions.
  • Without catalysts reactions take place too slowly to sustain biological life.
  • Enzymes are biological catalysts.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Enzymes and their Substrate

A

Enzymes act on a compound called a substrate
Highly specific-> each enzyme acts on a specific substrate only-> [called] specificity of enzymes (lock & key/induced fit)
Enzymes work by binding their substrate
Part of enzyme which binds to the substrate is called the ACTIVE SITE

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

What do Enzymes do?

A

Chemical reaction occurs if there is sufficient energy to begin the reaction
Enzymes reduce the amount of energy needed to begin a reaction- [important]
Enzymes reduce the Activation Energy

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

How do Enzymes work?

A
Two theories;
- The lock & key
- The induced-fit theory
Enzymes are not 'used up' in a reaction-> available for reuse (recycled in a cell)
pH & temperature can denature enzymes
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

The Lock-and-Key Theory

A

The substrate fits perfectly into the active site of the enzyme
- like a lock & key
{picture in PowerPoint}

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

The Induced-Fit Model

A

The shape of the active site varies slightly from the shape of the substrate and the substrate induces a change in shape of the active site so the two can fit together.
->Active sight varies to fit the substrate
{picture in PowerPoint}

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

Enzyme Theory

A

Why are there 2 theories/models to explain how enzymes work?
-Induced Fit = newer theory than the Lock & Key.

Which one do you think is the better theory/model that explains enzyme action?
-Induced Fit.

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

Factors Affecting Enzyme Activity

- TEMPERATURE

A

Denaturation- irreversible change in the protein structure resulting in permanent loss of protein function.
Enzymes have an OPTIMUM temperature range;
- temperatures between enzymes which activity is greatest
- most human enzymes have an optimal temperature of 37 degrees C
- heat-tolerant organisms (eg.bacteria) which live in hot springs have enzymes with higher optimal temperatures

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

Factors Affecting Enzyme Activity
- TEMPERATURE
(continued)

A

Critical temperature
-Temp at which denaturation of enzyme molecules begin to occur.

Lower temperatures
-Temporarily disrupt enzyme function but they do not denature the enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Factors Affecting Enzyme Activity

- pH

A

Optimal pH = enzyme shows maximal activity.
Enzymes Optimal pH = NEUTRAL or SLIGHTLY ACIDIC
Optimal pH of human enzymes will vary with the site of enzyme function;
- Pepsin - stomach, pH 2
- Trypsin - small intestine, pH 8
- Carbonic anhydrase - human blood, pH 7.4
- Human Cell enzymes, pH 7.6
A change in pH can alter the 3-D structure of the enzyme - reducing enzyme function

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

Affect of Concentrations

A

Enzyme Concentration
- if the amount of enzyme is increased, the amount of product produced per unit time increases…. as long as….
Substrate Concentration
- if the amount of substrate is increased, the amount of product produced per unit time increases…as long as…

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

Enzyme Inhibitors

A

Chemical substances can inhibit enzyme function by;
- Binding to the Active Site of the enzyme thus preventing substrate from binding (competitive inhibitor)
- Combining with another part of the enzyme in a way that the shape of the binding site is altered (non-competitive inhibitor)
{pictures in PowerPoint}

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

Enzymes and Diseases

A

Several inherited diseases are caused by the inability to manufacture a particular enzyme.

  • Galactosaemia -> error in the enzyme required to convert galactose.
  • Lactose Intolerance -> low levels of the enzyme lactose.
  • Phenylketonuria -> missing enzyme is phenylalanine hydroxlase.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Naming Enzymes

A

Normally an enzyme is named by attaching the suffix ‘-ase’ to the name of the substrate;
- (eg. CarbohydrASE, is an enzyme that acts on carbohydrates, lipASE acts on lipids, proteASE acts on proteins). - lactose (carbohydrate in dairy)-> lactASE, cellulose (plant cell walls)-> cellulASE
Naming rule NOT perfect*
- Trypsin & pepsin are both enzymes which act on proteins (they are proteASEs), but they were named before the rule came in.
- starch is digested by amylase?

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

Activation Energy

A

DEFINITION: Energy required to start a chemical reaction

16
Q

Structure of Enzymes

continued

A

Globular (round) protein

DEFINITION: the site on the surface of an enzyme that binds the substrate molecule

17
Q

Catabolic & Anabolic

FINISH STEPS INVOLVED & WHAT IS SPECIFICITY

A

Catabolic DEFINITION: breakdown of macromolecules into smaller molecules, releasing energy. (Exergonic)

Anabolic DEFINITION: building of larger molecules from smaller molecules, a process requiring energy to build new bonds. (Endergonic)

18
Q

Factors Affecting Enzyme Activity

-inhibitors

A

Inhibitors can inhibit enzyme function by:
Binding to the active site, therefore preventing the substate from binding. (Competitive inhibition)
Combining with another part of the enzyme, therefore the shape of the binding site is altered. (Non-competitive inhibition)

19
Q

Factors Affecting Enzyme Activity
-cofactors
FINISH

A

DEFINITION: Cofactor is a metallic cation required for proper function of enzyme.

Cofactors are additional non-protein part.
- includes: iron, calcium & zinc.

20
Q

Factors Affecting Enzyme Activity
-mutations
FINISH

A

Mutations

21
Q

Enzyme

A

DEFINITION: Protein that catalyses (increases the rate of) chemical reactions in living in living organisms. An enzyme is specific for a chemical reaction and may be used over and over again.

22
Q

Role of Enzyme in (PKU)

Phenylketonuria

A

Look up*

23
Q

Amount of reactants (substrate & product)

A

Substrate: more substrate present = move to the right ➡️

Product: more product present = move to the left ⬅️ (reactions slows)

24
Q

Building/Breaking Down Polymers: DEHYDRATION

A

Process adding each subunit involves removal of a molecule of water.

25
Q

Building/Breaking Down Polymers: HYDROLYSIS (water split)

A

Breakdown of polymers into subunits involves adding a molecule of water.