Session 11-Regulation of protein function Flashcards

1
Q

What are isoenzymes?

A

Different forms of the same enzyme that have different kinetic properties

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2
Q

True or false: accumulation of the product of a reaction inhibits the forward reaction

A

TRUE

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3
Q

Give an example of product inhibition

A

Glucose-6-phosphate inhibits hexokinase activity

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4
Q

What relationship do allosteric enzymes show between rate and substrate concentration?

A

Sigmoidal, rather than rectangular hyperbola seen for simple enzymes

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5
Q

Complete the sentence:

Substrate binding to one subunit makes subsequent binding to other subunits progressively ______

A

Easier

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6
Q

What do allosteric activators do?

A

Increase the proportion of enzyme in the R state

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7
Q

What do allosteric inhibitors do?

A

Increase the proportion of enzyme in the T state

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8
Q

True or false: phosphofructokinase is not allosterically regulated

A

FALSE - it is and it sets the pace of glycolysis

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9
Q

What are the allosteric activators for phosphofructokinase? (2)

A

AMP

Fructose-2,6-bisphosphate

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10
Q

What are the allosteric inhibitors for phosphofructokinase? (3)

A

ATP
Citrate
H+

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11
Q

What do protein kinases do?

A

Transfer the terminal phosphate from ATP to the -OH group of Ser, Thr and Tyr

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12
Q

What do protein phosphatases do?

A

Reverse the effects of kinases by catalysing the hydrolytic removal of phosphoryl groups from proteins

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13
Q

Why is protein phosphorylation so effective? (5)

A
  1. Adds two negative charges
  2. A phosphoryl group can make H-bonds
  3. Rate of phosphorylation/dephosphorylation can be adjusted
  4. Links energy status of the cell to metabolism through ATP
  5. Allow for amplification effects
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14
Q

Complete the sentence:

When enzymes activate enzymes, the number of affected molecules _________ _____________ in an enzyme cascade

A

Increases geometrically

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15
Q

What does amplification of signals by kinase cascades allow?

A

Amplification of the initial signal by several orders of magnitude within a few milliseconds

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16
Q

What does it mean by “glycogen breakdown and synthesis are reciprocally regulated”?

A

The signals that stimulate glycogen breakdown also inhibit glycogen synthesis

17
Q

Which enzyme catalyses glycogen breakdown?

A

Phosphorylase a

18
Q

Which enzyme catalyses glycogen synthesis?

A

Glycogen synthase

19
Q

How are many enzymes activated?

A

Specific proteolytic cleavage

20
Q

How are digestive enzymes synthesised by specific proteolysis?

A

They are synthesised as zymogens in the stomach and pancreas

21
Q

What are zymogens?

A

Inactive precursors - converted into an enzyme when activated by another enzyme

22
Q

How is blood clotting mediated?

A

By a cascade of proteolytic activations that ensures a rapid and amplified response

23
Q

How is apoptosis mediated?

A

By proteolytic enzymes, caspases, which are synthesised in an inactive form (procaspase)

24
Q

What do endogenous inhibitors do?

A

Regulate protease activity

25
Q

What binds to trypsin and stops its activity?

A

Pancreatic trypsin inhibitor

26
Q

What is an example of a protein that inhibits a range of proteases?

A

Alpha1-antitrypsin

27
Q

What are people with emphysema deficient in and what does this cause?

A

Alpha1-antitrypsin which leads to the destruction of alveolar walls by elastase

28
Q

What are the two types of short term protein regulation?

A
  1. Substrate and product concentration

2. Change in enzyme conformation (allosteric regulation, covalent modification and proteolytic cleavage)

29
Q

What are the two types of long term protein regulation?

A
  1. Change in rate of protein synthesis

2. Change in rate of protein degradation

30
Q

What is an example of enzyme induction/repression?

A

Alcoholics make more alcohol dehydrogenase

31
Q

Which enzyme catalyses the formation of a fibrin clot?

A

Thrombin

32
Q

Why is the intrinsic pathway more important than the extrinsic pathway of blood clot formation?

A

Once it starts, it is self-sustaining

33
Q

What are Gla domains?

A

Gamma-carboxyglutamate residues which are very negatively charged

34
Q

What do Kringle domains do?

A

Keep prothrombin in the inactive form

35
Q

How does Ca2+ play a role in blood clotting?

A

Interacts with damaged membranes and acts as a cross-bridge with Gla domains to allow for a quicker reaction

36
Q

Complete the sentences:

The newly formed clot is stabilised by the formation of _____ bonds between the side chains of ______ and _________ residues in different monomers. This cross-linking reaction is catalysed by _________________ which is activated from _________________ by thrombin.

A
Amide
Lysine 
Glutamine 
Transglutamine 
Protransglutaminase
37
Q

What is classic haemophilia a defect in?

A

Factor VIII

38
Q

What are two ways to stop the clotting process?

A
  1. Localisation of (pro)thrombin - dilution of clotting factors by blood flow and removal by liver
  2. Digestion by proteases
39
Q

How is the clotting process regulated? (1)

A

Specific inhibitors - antithrombin III (AT3)