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Flashcards in Enzyme Mechanism of Action Deck (34):
1

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

Quantity and activity

2

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.

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

3

What are four reasons enzymes are the preferred catalysts?

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

4

What are RNA enzymes called?

RNases or ribozymes

5

This enzyme types transfers electrons.

oxidoredcutase

6

This enzyme type transfers groups

transferase

7

This enzyme type removes a functional group with water.

hydrolase

8

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

lyase

9

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

isomerase

10

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

ligase
"Forms CONS bonds via CONdenSation and ATP"

11

What are nonprotein enzyme aids called?

Coenzymes, cofactors, prosthetic groups

12

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

part

13

What are two examples of cofactors in TCA?

NAD+, FAD

14

Many coenzymes are derivatives of...

vitamins

15

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

apoenzymes, holoenzymes

16

NAD+ is _____ while FAD is bound.

mobile

17

Can be derived from Trp in humans and vitamin B3

niacin

18

Describe the four types of enzyme catalysis.

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

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

High level of processing and keeps metabolites at high concentration

20

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

Induced fit: hexokinase and citrate synthase
Lock and key: dihydrofolate reductase

21

What are the differences between enzymes and isoenzymes?

Isoenzymes can have different reaction rates and inhibition rates.

22

What is the benefit of have isoenzymes?

backup in the body because have same function as general enzyme

23

Elevated levels of isoenzymes could indicate _____.

disease

24

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

LDH 5 is found in the muscles. Takes pyruvate to lactate.
LDH 1 is found in the heart. Takes lactate to pyruvate.

25

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

Covalent, acid

26

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

Beriberi
Derived from vitamin B1

27

Serum amylase suggests what illness?

Acute pancreatitis

28

What enzymes compose the PDH complex?

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

29

What are the prosthetic groups/coenzymes of PDH?

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

What does a dietary deficiency in niacin cause?

pellagra

31

Tetrahydrofolate (THF) deficiency can result in?

spinabifida

32

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

mutations in evolutionarily conserved residues

33

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

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

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

Transfers one carbon units on its N5