Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Elements of Medicine > Enzyme Mechanism of Action > Flashcards

Enzyme Mechanism of Action Flashcards

1
Q

Changes in the ____ and ____ of enzymes can be determined by blood tests.

A

Quantity and activity

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

Genetic defects, _____ deficits, ____ damage, the presence of toxins, the activity of bacterial/viral agents, and enzyme _____/____ all can lead to changes in enzyme activity and yield pathological conditions.

A

genetic defects, nutritional deficits, tissue damage, the presence of toxins, the activity of bacterial/viral agents, and enzyme inhibitors or activators

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

What are four reasons enzymes are the preferred catalysts?

A

Work at milder conditions, can be regulated, reaction specificity, increase reaction rates

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

What are RNA enzymes called?

A

RNases or ribozymes

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

This enzyme types transfers electrons.

A

oxidoredcutase

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

This enzyme type transfers groups

A

transferase

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

This enzyme type removes a functional group with water.

A

hydrolase

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

This enzyme types cleaves bonds via elimination (pi bond) or adds a group to a pi bond.

A

lyase

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

This enzyme type transfers groups within a molecule to yield isomers.

A

isomerase

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

This enzyme type forms C-C, C-O, C-N, C-S bonds via condensation and ATP.

A

ligase

“Forms CONS bonds via CONdenSation and ATP”

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

What are nonprotein enzyme aids called?

A

Coenzymes, cofactors, prosthetic groups

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

Prosthetic groups are different from cofactors because they are _____ of the enzyme.

A

part

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

What are two examples of cofactors in TCA?

A

NAD+, FAD

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

Many coenzymes are derivatives of…

A

vitamins

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

Enzymes without the necessary cofactors are called____. What is the opposite?

A

apoenzymes, holoenzymes

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

NAD+ is _____ while FAD is bound.

A

mobile

17
Q

Can be derived from Trp in humans and vitamin B3

A

niacin

18
Q

Describe the four types of enzyme catalysis.

A

Covalent: formation of a covalent intermediate with the substrate before the product is formed
Acid Base: group on enzyme acts as an acid or base, taking away or giving a H+ to the substrate.
Proximity: if substrate is available at high concentration and is close enough to the enzyme, a reaction will occur
Strain: enzyme binds the substrate in a statically unfavorable way to break the necessary bond

19
Q

What is the benefit of having 60 active site on PDH?

A

High level of processing and keeps metabolites at high concentration

20
Q

What are examples of the induced fit model and the lock and key model?

A

Induced fit: hexokinase and citrate synthase

Lock and key: dihydrofolate reductase

21
Q

What are the differences between enzymes and isoenzymes?

A

Isoenzymes can have different reaction rates and inhibition rates.

22
Q

What is the benefit of have isoenzymes?

A

backup in the body because have same function as general enzyme

23
Q

Elevated levels of isoenzymes could indicate _____.

A

disease

24
Q

Lactate DH has two main isoenzymes. What are they? What are their function? Where are they found?

A

LDH 5 is found in the muscles. Takes pyruvate to lactate.

LDH 1 is found in the heart. Takes lactate to pyruvate.

25
Q

Serine proteases often interact in _____ catalysis. Aspartate proteases (like in HIV) often interact in _____ catalysis.

A

Covalent, acid

26
Q

If thiamin pyrophosphate (TPP) is missing, what illness results?

A

Beriberi

Derived from vitamin B1

27
Q

Serum amylase suggests what illness?

A

Acute pancreatitis

28
Q

What enzymes compose the PDH complex?

A

E1: Pyruvate Dehydrogenase
E2: Dihydrolipoyl transacetylase
E3: Dihydrolipoyl dehydrogenase

29
Q

What are the prosthetic groups/coenzymes of PDH?

A 
TPP -bound to E1. Aldehyde transfer
Lipoate - covalently linked to E2. Aceyl group transfer
Coenzyme A - substrate for E2
FAD - bound to E3
NAD - substrate for E3-reduced by FADH2
30
Q

What does a dietary deficiency in niacin cause?

A

pellagra

31
Q

Tetrahydrofolate (THF) deficiency can result in?

A

spinabifida

32
Q

The majority of enzyme/protein based diseases are cause by—-

A

mutations in evolutionarily conserved residues

33
Q

NAD+(P)- dependent DH produce a fluorescent product. What how does this help with enzyme activity quantification?

A

340 nm is where NADPH absorbs. See how much NADPH there is to determine the enzyme activity.
Both (NAD (P) and NAD(P)H) absorb at 250 so don’t want to look at that portion of the absorbency spectrum

34
Q

What is tetrahydrofolate’s (THF) role in reaction?

A

Transfers one carbon units on its N5

Elements of Medicine (10 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions