Regulating Proteins Flashcards

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1
Q

What is an isoenzyme?

A

Different forms of the same enzyme(They catalyse the same reaction but have different kinetic properties)

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2
Q

What is product inhibition?

A

Accumulation of the product inhibits the forward reaction.

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3
Q

What is allosteric regulation?

A

Sigmoid relationship between rate and sub start e conc. Eg haemoglobin and oxygen- one bonded oxygen increases the affinity.

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4
Q

What is an alllosteric effector?

A

Something that binds to the enzyme away from the active sister which changes the state of the enzyme from its T state to its R state by giving conformational change.

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5
Q

What is an example of allosteric regulation

A

AMP and fructose-2 and 6-bisphosphate activate phosphofructokinase
ATP and H+ and citrate inhibit it.

This is a key regulator in glycolysis.

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6
Q

What’s the most common covalent modification to enzymes to help regulation?

A

Phosphorylation

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7
Q

Which enzyme phosphorylated and what enzyme reverses this.

A

Protein kinases transfer a phosphate from ATP to the -OH on SER, THR and TYR
Protein phosphates reverse this by hydrolysis removal of a phosphoryl group

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8
Q

What is a zynogen?

A

Digestive enzymes.

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9
Q

What stimulates the intrinsic pathway?

A

Damaged endothelial lining of blood cells stimulates binding of factor 12.

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10
Q

In blood clotting what stimulates the external pathway?

A

Trauma releases tissue factor

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11
Q

What is a peptidase?

A

Something that cuts up peptide bonds

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12
Q

How do we stop clotting so al the circulating blood doesn’t clot?

A

Localisation of thrombin, get more dilute and are removed by the liver.
Digestion by Proteases eg Protein C is activated my thrombin when at a certain level and they breaks down some clotting factors.

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