Chapter 8.5.3 (Exam 2) Allostery Flashcards

Enzyme Activities Can Be Regulated

1
Q

Describe the reaction rate in allosteric enzymes.

A

very sensitive to substrate concentration (over a certain range)

very sensitive to low concentrations of inhibitors

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2
Q

What is the commitment step in metabolic pathways?

A

The first reaction, the other reactions happen in sequence

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3
Q

What happens in a metabolic pathway if the cell no longer requires the product?

A

Feedback inhibition: The final product usually acts as a noncompetitive inhibitor of the first enzyme, which shuts down the pathway

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4
Q

What is the function of reverse phosphorylation?

A

Regulating enzymes: enzymes can be activated when protein kinase adds a phosphate group and deactivated by protein phosphatase removing a phosphate group

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5
Q

What is the function of a protein kinase in enzyme phosphorylation?

A

Enzymes can be activated when protein kinase adds a phosphate group

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6
Q

What is the function of a protein phosphatase in enzyme regulation?

A

Enzymes can be deactivated by protein phosphatase removing a phosphate group

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7
Q

Why is enzyme function dependent on pH?

A

Differing pH can ionize or deionize functional groups, changing enzyme shape and the different substrate it may fit

E.g. at low pH (high H+) —COO– may react with H+ to form —COOH which is no longer charged; this affects folding and thus enzyme function.

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8
Q

Why does every enzyme have an optimal temperature?

A

At high temperatures, noncovalent bonds begin to break, breaking down tertiary structure and causing denaturation

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9
Q

Which bonds are more present in enzymes that are adapted to warmer temperatures?

A

Covalent bonds because they are stronger

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10
Q

Why does the human body fight infections with fevers?

A

Most human enzymes are stable at high temperatures compared to bacterial enzymes

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