Enzymen

Question 1

What are the main classes of enzymes?

Answer 1

The main classes of enzymes are oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.

Question 2

True or False: Enzymes are only involved in the breakdown of substrates.

Answer 2

False: Enzymes can also facilitate the synthesis of substrates.

Question 3

Fill in the blank: Enzymes that catalyze oxidation-reduction reactions are called __________.

Answer 3

oxidoreductases

Question 4

Which class of enzyme transfers functional groups from one molecule to another?

Answer 4

Transferases

Question 5

What type of enzyme is responsible for hydrolysis reactions?

Answer 5

Hydrolases

Question 6

Multiple Choice: Which of the following is NOT a class of enzymes? A) Ligases B) Synthases C) Hydrolases D) Isomerases

Answer 6

B) Synthases

Question 7

What is the function of lyases?

Answer 7

Lyases catalyze the addition or removal of groups to form double bonds.

Question 8

True or False: Isomerases change the configuration of a molecule without adding or removing anything.

Answer 8

True

Question 9

What class of enzyme joins two molecules together?

Answer 9

Ligases

Question 10

Fill in the blank: Enzymes are biological __________ that speed up chemical reactions.

Answer 10

catalysts

Question 11

Wat zijn diverse enzymen?

Answer 11

Lipase, Protease, Amylase, Stremsel, lysozym, lactase

Question 12

Wat is de rol van protease?

Answer 12

Het afbreken van eiwit

Question 13

Wat is de rol van lipase?

Answer 13

Het afbreken van vet

Question 14

Wat is de rol van lysozym?

Answer 14

Is een conseveermiddel

Question 15

Wat is het nut van lactase?

Answer 15

Voor lactose arm melk

Question 16

Welke Co-enzymen heb je?

Answer 16

Co-substraten: NAD/NAHD, CoA en ATP.
Protetische groep: Heem groep

Question 17

Welke essentiele ionen heb je?

Answer 17

Activator ionen en metaal ionen.

Question 18

Welke soorten enzym remmers heb je?

Answer 18

Irriversible, reversible waaronder competitief, oncompetitief, niet-competitief en gemengd.

Question 20

What effect does competitive inhibition have on Vmax?

Answer 20

Vmax remains unchanged.

Question 21

What happens to Km in the presence of competitive inhibitors?

Answer 21

Km increases.

Question 22

True or False: Non-competitive inhibition affects Vmax but not Km.

Answer 22

True.

Question 23

What is the effect of non-competitive inhibition on Vmax?

Answer 23

Vmax decreases.

Question 24

How does non-competitive inhibition affect Km?

Answer 24

Km remains unchanged.

Question 25

Fill in the blank: In competitive inhibition, the binding of the inhibitor is ______ to the active site.

Answer 25

reversible.

Question 26

What type of inhibition involves an inhibitor binding to an allosteric site?

Answer 26

Non-competitive inhibition.

Question 27

In the context of enzyme inhibition, what does Km represent?

Answer 27

The substrate concentration at which the reaction rate is half of Vmax.

Question 28

What is the primary characteristic of non-competitive inhibitors?

Answer 28

They can bind to the enzyme whether or not the substrate is bound.

Question 29

Which type of inhibition can be overcome by increasing substrate concentration?

Answer 29

Competitive inhibition.

Question 30

True or False: In non-competitive inhibition, increasing substrate concentration has no effect on Vmax.

Answer 30

True.

Question 31

What happens to the slope of the Lineweaver-Burk plot in competitive inhibition?

Answer 31

The slope increases.

Question 32

Complete the sentence: In competitive inhibition, the inhibitor competes with the substrate for the ______.

Answer 32

active site.

Question 33

What is the effect of uncompetitive inhibition on both Vmax and Km?

Answer 33

Both Vmax and Km decrease.

Question 34

True or False: Non-competitive inhibitors can affect the maximum rate of reaction regardless of substrate concentration.

Answer 34

True.

Question 35

What does an increase in Km indicate about the affinity of the enzyme for the substrate in competitive inhibition?

Answer 35

The affinity decreases.

Question 36

In which type of inhibition is the inhibitor not affected by substrate concentration?

Answer 36

Non-competitive inhibition.

Question 37

What is the result of increasing substrate concentration in non-competitive inhibition?

Answer 37

No change in Vmax.

Question 38

What is the effect of competitive inhibition on enzyme activity at high substrate concentrations?

Answer 38

Enzyme activity approaches Vmax.

Question 39

Fill in the blank: Competitive inhibitors often resemble the ______ of the enzyme.

Answer 39

substrate.

Question 40

What happens to Vmax in mixed enzyme inhibition?

Answer 40

Vmax decreases.

Question 41

True or False: Km increases in mixed enzyme inhibition.

Answer 41

True.

Question 42

Fill in the blank: In mixed enzyme inhibition, the effect on Km is typically _____ or _____ depending on the inhibitor.

Answer 42

increased or decreased.

Question 43

What is the effect of mixed enzyme inhibition on the Lineweaver-Burk plot?

Answer 43

It results in that the intersect at the Y-as deceases and the intersect on the X-as meer naar rechts gaat. ines that intersect at a point left from the y-axis.

Question 44

Multiple Choice: In mixed enzyme inhibition, which of the following statements is true? A) Vmax increases, B) Km decreases, C) Vmax decreases and Km can increase or decrease, D) None of the above.

Answer 44

C) Vmax decreases and Km can increase or decrease.

Question 45

Wat zijn alle vormen van enzym regulatie?

Answer 45

n enzym, substraat en product. Homo- en hetro allosteren, covalente modificatie en feebackloop

Question 46

Wat zijn twee vormen van covalante modificatie

Answer 46

Enzym wordt pas actief na afknippen N-terminaal peptide (pro-enzym of zymogeen) ATP fosfaatgroep bind reversible aan -OH van Ser, Thr of Tyr

Question 47

Wat houd homo-allosterie in?

Answer 47

Ligand bind aan subunit van enzym. Vergemakkelijkt binding substraat aan enzym. Werkt voornamelijk geod bij hoge substraat concentraties

Question 48

Wat houd hetro-allosterie in?

Answer 48

Metabole remmers of activators binden aan het enzym. Activator + enzym = R vorm. Remmer + enzym = T vorm.

Question 49

Wat geeft Kcat (turnovergetal) aan?

Answer 49

n substraat per seconde omgezet. Kcat = Vmax/[E]tot