Regulatory Enzymes Flashcards

1
Q

How do enzymes work?

A

reactions take place in the active site which has high affinity for substates. active site provides an environment conducive to the reaction, bind to substates transition state

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

What curve is Michaelis Menten?

A

hyperbolic

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

What is a regulatory enzyme?

A

most enzymes are not regulatory. usually catalyze reactions that are:
-early in the pathway
-immediately after branch points
-far from equilibrium

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

What are the mechanisms of enzymes?

A

Rapid regulation:
-allosteric enzymes
-covalent modification
Slower:
-altered enzyme concentrations (changes in gene expresion, degradation)

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

What is an allosteric enzyme?

A

a change in the shape and activity of an enzyme that results from molecular binding with a regulatory substance at a site other than the active site

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

What is an example of an allosteric enzyme?

A

feedback inhibition- most studied
ATCase inhibition

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

What kind of kinetics does an allosteric enzyme show?

A

sigmoid kinetics, no Km (K0.5)

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

What are the 2 classes of allosteric regulation?

A

Homotropic: regulator is usually the substrate, binding to the active site increases the activity of the other active sites
Heterotrophic: modulators are generally metabolites or other small molecules, bind somewhere distinct to the active site

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

What are the two conformations of cooperativty?

A

T-state: low activity, stabilized by inhibtors
R-state: high activity. stabilized by activators

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

What are the 2 models of cooperativity?

A

-concerted: all subunits either in T or R state, oxygen shifts equillirium
-sequential: binding of oxygen causes a conformational change shifting T to R-state

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

What is regulation by covalent modification?

A

Phosphorylation! FAST!
Kinases- add phosphate
Phosphatase: remove phosphate

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

Explain phosphorylation.

A

Usually on a serine, threonine, sometimes tyrosine
hydroxyl is the phosphorylation site
can be complex

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

What is altered gene expression?

A

-transcription of specific genes regulated by numerous transcription factors
-can alter concentration of enzymes and other proteins
-transcription factors bind to promoters to regulate transcription
-complex and SLOW
ex: PEP carboxykinase

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