Biothermodtynamics DAT Booster

0.0(0)
Studied by 0 people
call kaiCall Kai
Locked
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
GameKnowt Play
Card Sorting

1/46

encourage image

There's no tags or description

Looks like no tags are added yet.

Last updated 6:02 PM on 7/17/26
Name
Mastery
Learn
Test
Matching
Spaced
Call with Kai
Chat

No analytics yet

Send a link to your students to track their progress

47 Terms

1
New cards

_____ describes when a cofactor is covalently bound to an enzyme.

Prosthetic group

2
New cards

______ experiences cooperativity.

Hemoglobin

3
New cards

If Km value of an enzyme is elevated, then the _____.

substrate does not bind to the enzyme well

4
New cards

Km is the ______.

Substrate concentration at half of the maximum rate of a catalyzed reaction

5
New cards

A drug can inhibit a substrate by mimicking its structure & binding to its enzyme’s active site. What is occurring?

competitive inhibition

6
New cards

In order to counteract competitive inhibition, what can be done?

Increase substrate concentration

7
New cards

What occurs during competitive inhibition of an enzyme?

  • Substance mimics a substrate and inhibits the enzyme by binding at the active site

  • Vmax is unchanged

  • Km increases

8
New cards

What occurs during non-competitive inhibition of an enzyme?

  • inhibitor binds to enzyme’s allosteric site, reaction does not get catalyzed

  • Vmax decreases

  • Km is unchanged

9
New cards

Which biological molecule makes up enzymes?

Amino acids

10
New cards

If biding affinity is high, then Km is ____.

low

11
New cards

Vmax is the ___.

max rate of an enzyme catalyzed reaction

12
New cards

If Km value of an enzyme is low, what is occuring?

Enzyme requires a relatively low substrate concentration to reach ½ Vmax

13
New cards

If a reaction has a +^G value, then _____.

  • the reaction is endergonic (require an input of energy to occur)

  • the reaction in non spontaneous

14
New cards

The ability to drive a secondary active transport can be explained by _____.

Gibbs free energy

15
New cards

What is an example of how potential energy is stored in the biological systems?

The chemical bonds b/w phosphate groups in an ATP molecule

16
New cards

How are non-spontaneous reactions driven forward in biological systems?

Reaction coupling

17
New cards

True or false: ATP’s bonds b/w its phosphate groups are high energy

True

18
New cards

True or false: ATP can be used to power non-spontaneous chemical reactions

True

19
New cards

True or false: ATP is a nucleotide

True

20
New cards

True or false: ATP hydrolysis is a highly endergonic reaction

False

21
New cards

True or false: The formation of ATP from ADP requires energy to occur

True

22
New cards

True or false: Catalysts can lower the activation energy of the reaction

True

23
New cards

True or false: Catalysts can stabilize the transition state

True

24
New cards

True or false: Catalysts can make non-spontaneous reactions spontaneous

False

25
New cards

True or false: Catalysts can provide an alternative pathway

True

26
New cards

True or false: Catalysts can be reused, as they are not consumed in the reaction

True

27
New cards

Enzyme-substrate complexes are held together via_____.

Weak, temporary bonds

28
New cards

What best describes cofactors and how they are involved in enzyme catalysis?

Cofactors can bind covalently or non-covalently to the enzyme

29
New cards

True or false: Zymogens help with enzyme regulation

True

30
New cards

True or false: All zymogens are proenzymes

True

31
New cards

True or false: Zymogens can be activated through cleavage

True

32
New cards

True or false: Zymogens are active biological catalysts

False

33
New cards

Pepsinogen is a zymogen found in the human stomach

True

34
New cards

What effects enzyme function and regulation?

pH, chemical modification, temperature, gene expression

35
New cards

What does not effect enzyme function and regulation?

free energy

36
New cards

How can the Vmax of an enzyme can be increased?

Increasing the enzyme concentration

37
New cards

What may affect the Km of an enzyme?

Competitive inhibition

38
New cards

What decreases the Vmax of an enzyme?

Non-competitive inhibition

39
New cards

What is true regarding the Gibbs free energy of cellular respiration?

^H-T^S has ne negative value (makes a reaction favorable)

40
New cards

ATP is an unstable molecule because ____.

it has 3 negatively charged phosphate groups

41
New cards

What is Q10?

It measures how sensitive reaction rates are to temperature changes

42
New cards

Q10 temperature coefficient equation

Q10 = (K2/K1)^(10/t2-t1)

43
New cards

Examples of hydrolases

  • Lipase

  • Peptidase

  • Nuclease

  • Amylase

44
New cards

_____are enzymes that break down molecules using water (via hydrolysis).

Hydrolases

45
New cards
  • Chymotrypsin

  • Pepsin

  • Trypsin

All of these enzymes are involved in protein digestion

46
New cards

____ is an enzyme that is responsible for breaking down starch into maltose.

Amylase

47
New cards

A researcher needs to cut a circular plasmid at a specific DNA sequence in the middle of the strand. What enzyme should be used to make this cut?

Endonuclease