Structure and Function Flashcards

1
Q

What are materials with Catalytic Properties and increase the rate of reactions?

A

Enzymes

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

What is a Constitutive Enzyme?

A

One that is always present and functioning

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

What is an Inducible Enzyme?

A

One that is produced in response to stimuli
Must be called on

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

Where can Cellular Enzymes be dissolved?

A

Cytoplasm
Microsomes/Mitochondria/Nuclei/Lysosomes

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

What is an Enzyme made of?

A

Carbon, Hydrogen, Oxygen, Nitrogen, and Sulfur

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

How de we tell Enzymes apart from one another?

A

Catalytic Action

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

What does each Enzyme contain?

A

An Active and Allosteric Site

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

What is the term used for Enzymes that perform the same function but come in different forms?

A

Isoenzymes or Isozymes

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

What is the nonprotein substance that attaches to an Enzyme known as?

A

A Cofactor

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

What can remove a Cofactor from an Enzyme?

A

Dialysis

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

What are the Organic Cofactors and what are they known as?

A

NADP+ and P5P
Known as Coenzymes

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

What are the Inorganic Factors and what are they known as?

A

Inorganic Ions like Cl- and Mg2+
Known as Activators

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

What are the different classifications of Enzymes?

A

Oxidoreductase (Redox reactions)
Transferase (Transfer functional groups)
Hydrolase (Breaking bonds with water)
Lyases (Add or remove double bonds)
Isomerases (One isomer to another)
Ligases (Making or breaking bonds)

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

What is the study of Enzyme reaction rates?

A

Enzyme Kinetics

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

What is Enzyme Specificity?

A

Enzyme’s ability to bind to one or a few substrates

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

What are the types of Enzyme Specifities?

A

Absolute (One substrate)
Group (Same functional group)
Linkage (Form or break certain bonds)
Stereochemical (One Enantiomer from the other)

17
Q

What is First Order Kinetics?

A

Reaction rate is directly proportional to Substrate Concentration

18
Q

What is Zero Order Kinetics?

A

Reaction rate only depends on Enzyme Concentration
Peak reaction velocity

19
Q

What pH do enzymes perform best at?

20
Q

What can cause reaction rate to decrease?

A

Change in pH
More basic or acidic
Result in Denaturation

21
Q

An enzymes temperature is 10C. How will it perform?

A

Remain stable

22
Q

An enzyme temp is 41C. How will it perform?

A

It will collide and vibrate more causing denaturation

23
Q

What can bind to an Enzyme to reduce its Catalytic ability?

A

Inhibitors

24
Q

How are inhibitors classified?

A

Competitive or Noncompetitive

25
How do Competitive Inhibitors function?
Inhibitors resemble the substrate Bind to the active site
26
How do Noncompetitive Inhibitors function?
Binds to a place other than the active site (Allosteric site) Irreversible
27
What is the difference between Noncompetitive and Uncompetitive Inhibition?
Uncompetitive Inhibition binds to the Enzyme Substrate complex and not the free Enzyme
28
What is Enzyme Quantitation?
Measuring Enzyme catalytic activity Activity is related to concentration
29
What are the methods of Enzyme Quantitation?
Fixed Time Continuous Monitoring
30
Fixed Time Method
Reactants are combined for a certain time then stopped The larger the reaction, the more the Enzyme is present
31
Continuous Monitoring Method
Measures absorbance change at specific time intervals Continuous Recording Spectrophotometer
32
Why is the Continuous method preferred over Fixed Time?
Linearity of reaction can be better verified Deviation of linearity is readily observable