Enzymes lecture 5 Flashcards

1
Q

The product of one enzyme controlled reaction becomes the ____ of the next reaction

A

Substrate

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

Regulatory enzymes are the enzymes that have a GREATER OR LESSER? effect on the overall rate of the sequence of reaction

A

Regulatory Enzymes

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

These enzymes exhibit changes in catalytic activity in response to certain signals

Their activity is controlled by interactions with ____-

A

Regulatory Enzymes

Other molecules

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

What are the 4 things that can accomplish regulation?

A

Small molecules (metabolites/cofactors)

Other proteins that bind to the enzyme

Covalent modification of enzyme

Zymogen is cleaved to form the active enzyme

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

The activity of regulatory enzymes have be controlled by small molecules such as ____ or ____

They act as ____ effectors or ______ modulators

A

Metabolites or cofactors

Allosteric effectors

Allosteric Modulators

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

What type of binding occurs with small molecules in enzymes like metabolites and cofactors?

What does it do the enzyme?

A

Noncovalent

Change its shape (more active or inhibited)

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

No allosteric enzymes follow M-M kinetics?

What dependence do they show?

A

No

Sigmoidal

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

Allosteric behavior (with small molecules) is observed in what type of proteins?

A

Multisubunits having quaternary structure

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

The modulator in allosteric effectors is often the substrate itself, when substrate and modulator are identical the regulatory enzyme is ___

A

Homotropic

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

A hypothetical enzyme has two identical subunits, each containing an active site. Each sub unit has a _____ state and ____ state conformation

When a substrate binds to one subunits, there is a change from ___ to _____

What does this do for affinity of substrate binding?

A

T and R state

T to R conformation

increases the affinity for substrate binding and reaction velocity

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

If a modulator and substrate are different, the enzyme is ___

An allosteric effector molecule OTHER than the substrate can also bind to the enzyme to inhibit or activate the enzyme by stabilizing the T or R state

Binding of the modulator triggers _____, the substrate can now bind the substrate with higher or lower affinity

A

Heterotropic

Triggers a conformational change

It can bond with greater affinity

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

This is an allosteric enzyme with 12 polypeptide chains organize into catalytic and regulatory subunits

It catalyzes the formation of N-carbamoylaspartate from ____ and ____

This reaction is the first step in a sequence of rxns which leads to the synthesis of ______ nucleotide, UMP a

A

Asptartate Transcarbamoylase

Aspartate and carbamoyl phosphate

Pyrimidine nucleotide, UMP

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

UMP can be converted by UTP to _____

It can then by aminated by ____ to give CTP

A

ATP

Glutamine

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

____ is an activator in bacteria

____ is an inhibitor of aspartate transcarbamoylae

A

ATP

CTP

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

The regulation by CTP is an example of ________

A

Feedback inhibition

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

Enzyme can also be controlled by other ___ which bind to the enzyme and activate or inhibit it by changing its conformation

The activity of Ca(2+)-ATPase is regulated by the protein ____

A

Proteins

Calmodulin

17
Q

What does Ca(2+)-ATPase do in cells?

It’s coupled by hydrolysis of

A

Catalyzes the transport of Ca across cell membranes

ATP

18
Q

The binding of Ca2+ to calmodulin causes a ____ in the protein

Ca2+ calmodulin activates _____ by binding to the enzyme which causes a change in its structure

A

Conformational Change

Ca(2+)-ATPase

19
Q

Enzyme activity can be regulated by ___ modification of the enzyme molecule

What is the most common type of regulatory modification?

A

Covalent

Phosphorylation

20
Q

What residues of an enzyme can be phosphorylated

What does it?

It can change the TERTIARY structure of an enzyme from __ to ____ or vice versa

A

Ser, Thr, Tyr (the ones with hydroxyl groups)

A protein kinase

Active to inactive, vice versa

21
Q

Enzyme activity can be regulated when a _____ is cleaved to form the active enzyme

____ and ___ are initially synthesize as inactive precursors chymotrypsinogen and
trypsinogen.

A

Zymogen

22
Q

This is an inactive precursor or proenzyme

A

Zymogen

23
Q

What type of reaction converts Chymotrypsinogen into π-chymotrypsin?

What about converting trypsinogen to trypsin?

A

Hydrolysis

Hydrolysis

24
Q

Do some regulatory enzymes use several regulatory mechanisms?

A

Yes