Enzyme Regulation Flashcards

1
Q

What are four ways of regulating enzyme activity?

A

Association with a regulatory protein

Sequestration (compartmentation)

Allosteric Regulation

Covalent Modification

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2
Q

How does compartmentalization regulate enzyme activity?

A

Isolating the reaction substrate or product from competing reactions

Provides a favorable environment

E.g. Acetyl-CoA carboxylase

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3
Q

What are some properties of enzymes that allow them to be regulated?

A

-pH, Km

Availability of substrate

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4
Q

What is feedback inhibition?

A

First enzyme in a multi-step pathway inhibited by the final product of the pathway

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5
Q

What is allosteric regulation?

A

Binding of small molecules that can increase or decrease activity of the enzyme

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6
Q

What is a homotropic allosteric regulator?

A

An allosteric regulator of the enzyme that is also a substrate for the enzyme.

(E.g. oxygen for hemoglobin)

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7
Q

What is a heterotropic allosteric regulator?

A

Regulatory molecule that is not the enzyme’s substrate.

E.g. CTP and ATP for aspartate transcarbomylase

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8
Q

What type of V vs. [S] curve is displayed by allosteric enzymes?

A

Sigmoidal

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9
Q

What are the allosteric inhibitors and activators of aspartate transcarbamoylase?

A

CTP, an end product, inhibits it

ATP activates it

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10
Q

How do covalent modifications regulate metabolic flow?

A

Post translational modifications can activate or inhibit key metabolic enzymes.

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11
Q

What are two important types of regulatory modifications?

A

Phosphorylation and Acetylation

These are often reversible

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12
Q

What are three advantages to using post translational modification as a regulatory mechanism?

A

Rapid

Does not require new protein synthesis or degredation

Easily reversible

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13
Q

What are the target residues for phosphorylation?

A

Serine

Threonine

Tyrosine

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14
Q

What is the significance about the addition of a phosphate group during phosphorylation?

A

It adds two negative charges to the amino acid residue.

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15
Q

What is the function of lysine acetyltransferases?

A

Catalyze the transfer of the acetyl group of Acetyl-CoA to the e-amino groups of lysyl residues.

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16
Q

What is the significant change in acetylation?

A

Neutralize the positive charge on lysine residues

17
Q

What is SIRT3?

A

Major mitochondrial NAD+-dependent deacetylase involved in tumor suppression as well as many other physiological processes

18
Q

What are three characteristics of proteolysis?

A

Irreversible

Near ubiquitous

Rapid mobilization of an activity in response to physiologic demand

19
Q

What are three ways proteolysis occurs?

A

Methionine excision - removal of first Met after translation

Signal peptide removal

N- and C-terminal processing