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Bio 204 > Enzymes > Flashcards

Enzymes Flashcards

1
Q

Thermodynamics doesn’t adress

A

Reaction speed

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2
Q

Table sugar breakdown

A

No reactions in the bag, it does in the cells because there are enzymes present

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3
Q

Chemical reaction occur when

A

Bonds are broken or established

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4
Q

Activation energy (Ea)

A

The initial energy investment required to start a reaction

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5
Q

Transition state

A

The necessary Ea was gained. Bonds are unstable and ready to be broken

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6
Q

What provides Ea

A

Particles natural movement or one reaction provides energy for another

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7
Q

Too much energy

A

Creates to much movement, leading to too much heat, which causes too many reaction and there is often burning (propane)

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8
Q

Why biology cannot use heat as Ea

A

Heat destroys the cell (specifically proteins) by destroying the structure
All reactions in the cell would start, killing the cell

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9
Q

Catalyst

A

Used in biology. A chemical agent that speeds up a reaction without taking part in it.

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10
Q

The most common catalyst

A

Enzymes

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11
Q

Importance of the transition state

A

A kinetic barrier as only some molecules have enough energy to react. Allows reactions to go one at a time

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12
Q

Enzymes job

A

Lower the transition state so more molecules can react. The do not alter thermodynamics or provide energy for a reaction

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13
Q

Substrates

A

The reactant an enzyme works on

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14
Q

Enzyme specificity

A

Each enzyme can only catalyze one of a couple similar molecules. This is why there are many enzymes per cell

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15
Q

Active site

A

The location on the enzyme where the catalysis takes place. A grove is formed when the protein folds, a very small section of the enzyme

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16
Q

Lock and key theory

A

Substates (keys) use the lock (Enzyme) to unlock the door (start a reaction) this is an old theory from the 1900’s

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17
Q

Induced fit hypothesis

A

Current view on enzyme function. Before a substrate bonds an enzyme goes though conformation so the active site is the most precise shape

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18
Q

Conformation

A

The process of an enzyme changing shape

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19
Q

Enzyme cycle

A

The process of grabbing substrates, catalyzing them, releasing them…

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20
Q

Cofactor

A

A non protein group that binds to an enzyme. Often a metal in which very little is required for catalysis

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21
Q

Cofactor metals

A

Fe, Cu, Zn, Mn

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22
Q

Coenzyme

A

A cofactor made of organic molecules, often derived by a vitamin

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23
Q

3 ways enzymes lower Ea

A

Bring reactant molecules together
Exposing the molecule to altered changed environments
Changing the shape of the substrate molecule

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24
Q

Bring reactant molecules together

A

Makes them collide in the right orientation so there is a reaction

25
Q

Exposing the molecule to altered changed environments

A

Active sites may contain ionic group with positive or negative charges

26
Q

Changing the shape of the substrate molecule

A

Strain the molecule into a conformation that mimics the transition state

27
Q

Without enzymes

A

Reactions would still happen, just not frequently

28
Q

Factors that effect enzyme activity

A

Substrate and molecule concentration, temperature, pH

29
Q

Common way to study enzymes

A

Rate of reaction by the enzyme and how it changes in response to experimental parameters

30
Q

Procedure

A

Purify the enzyme from the cell, incubate it in a buffered solution, five the reaction a substrate, look at the rate of the product being formed

31
Q

Excess substrate

A

Rate of catalysis is proportional to the amount of enzyme. The amount of enzymes limits the reaction

32
Q

Constant enzyme concentration- low to high concentration

A

Low- few collisions, few reactions
As it increases it is linear until the maximum amount of an enzyme can be catalysis is reached. Then concentration has no effect

33
Q

Saturated with substrate

A

When the catalyic cycle is going as fast as possible

34
Q

Competitive regulation (competitive inhibition)

A

When molecules that resemble substrates, and substrates fight for the same active sight

35
Q

Strength of competitive regulators

A

Some are covalently bonded, strong and irreversible

Non covalent bonds are weaker and reversible, can be overcome by high substrate concentration

36
Q

Cyanide

A

An inhibitor that prevents cellular respiration.

37
Q

Drugs are..

A

both helpful and harmful inhibitors

38
Q

Non competitive regulation

A

Competitors interact with the parts of the enzyme that are not the active site. Can increase of decrease enzyme function

39
Q

Allosteric site

A

A irreversible bond on this site controls enzyme activity

40
Q

Allosteric enzyme

A

An enzyme controlled by a allosteric site. Can have a high or low affinity state

41
Q

High affinity state

A

Enzyme binds strongly to the substrate

42
Q

Low affinity state

A

Enzyme binds weakly to the substrate

43
Q

Allosteric inhibitor

A

Converts an enzyme from high to low affinity

44
Q

Allosteric activator

A

Converts an enzyme from low to high affinity

45
Q

How cell reactions are controlled

A
  1. Abundance of specific enzymes
  2. Allosteric control
  3. Covalent modification
46
Q

Abundance of specific enzymes

A

The amount of enzymes is regulated by gene expression (only how many is needed is made). Can take up to 30 minutes

47
Q

Allosteric inhibitors are…

A

A form of feedback inhibition

48
Q

Feedback inhibition

A

If too much of a product is made, it becomes an inhibitor for its own reaction. When not enough is present the inhibitors leave and the reaction starts again

49
Q

Multi step feedback inhibition

A

The product inhibits the production of the starting product to avoid wasting intermediate products

50
Q

pH of enzymes

A

Each function in a specific pH and the farther from their optimum the less they work. Outside of the range the charge groups differ (H+ and OH- concentration)

51
Q

Most enzymes pH

A

7 because that is what cells sit at

52
Q

Pepsin

A

An enzyme with a ideal pH of 1.5 because it lives in the stomach

53
Q

Trypsin

A

An enzyme with an ideal pH of 8 because it lives in the small intestine

54
Q

Effects of temperature

A
  1. Reactions naturally increase as temp increases

2. With more, stronger collisions enzymes may become dismembered

55
Q

Denaturation

A

The enzyme unfolding. Occurs when the amino acids start moving and more collisions in high heat.

56
Q

0-40 c

A

Reaction rate doubles for every 10 increase

57
Q

Above 40

A

Denaturation causes a level peak, then falls to 0.

58
Q

Most enzymes peak temperature

A

40-50, and drop around 45-55

59
Q

Corn enzymes

A

Peak at 30 and is harmed above that. Hot days are bad for corn

Bio 204 (23 decks)

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