Enzyme Kinetics Flashcards

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1
Q

What is a catalyst?

A

A catalyst is a molecule that increases the rate in a chemical reaction without themselves being changed in the process.

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2
Q

Enzymes lower the ___________ of a reaction.

A

Activation energy

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3
Q

The _________ of an enzyme is where catalysis takes place.

A

Active Site

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4
Q

Bound metal ions can help __________ or can be a powerful driving force in ____________

A

position the substrate; oxidation-reduction reactions

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5
Q

In general acid-base chemistry, the amino acid side chain of an enzyme can donate or accept _________ to stabilize transitions states.

A

Protons

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6
Q

When cofactors or coenzymes are tightly bound to an enzyme, it is called a ____________

A

Prosthetic group

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7
Q

The velocity of a given enzymatic reaction depends on __________

A

The amount of substrate

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8
Q

Km is the amount of substrate needed for the enzyme velocity to be at __________

A

1/2Vmax

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9
Q

Kcat is the number of substrate molecules converted to product in a given unit time for a given enzyme molecule when ____________

A

The enzyme is saturated with substrate

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10
Q

The __________ the number from the ratio of Kcat/Km, the closer to enzymatic perfection

A

Larger

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11
Q

What are the three types of reversible inhibitors?

A
  1. Competitive 2. Uncompetitive 3. Mixed
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12
Q

A competitive inhibitor binds only to the ________ and not to the _________ and competes with the substrate for the __________

A

Enzyme, enzyme-substrate complex, active site

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13
Q

A competitive inhibitor _________ Km.

A

Increases

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14
Q

An uncompetitive inhibitor binds to the enzyme in a place other than the __________ and only to the _________

A

Active site; enzyme-substrate complex

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15
Q

Uncompetative inhibitors ________ Vmax

A

decreases

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16
Q

Mixed inhibitor binds outside the ________ but can bind to either the ________ or __________

A

Active site, Enzyme; Enzyme-Substrate complex

17
Q

Penicillin is an example of an ____________

A

Irreversible inhibitor

18
Q

Allosteric regulation of an enzyme

A

Binding of another molecule changes the conformation of the enzyme and alters function; usually involves feedback loops

19
Q

Covalent modification of an enzyme

A

Involves phosphorylation and is in response to intra/extra cellular signals

20
Q

Proteolytic cleavage on an enzyme

A

Once an enzyme is cleaved into a smaller segment, it is activated

21
Q

What are the four types of enzymatic regulators?

A

Allosteric, Covalent, Binding of another regulatory protein, Proteolytic cleavage