ai Flashcards

1
Q

What technique is most widely used to determine the 3D structure of enzymes?

A

X-ray crystallography

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2
Q

What does trypsin cleave on?

A

The carboxyl side of Arg or Lys

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3
Q

What specific bonds does thrombin cleave?

A

Arg-Gly bonds in particular sequences

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4
Q

What determines the specificity of an enzyme?

A

The 3D-structure of the enzyme

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5
Q

What are cofactors?

A

Metal ions or organic molecules

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6
Q

What role do many coenzymes serve in enzymatic reactions?

A

Intermediate carriers or functional groups in conversion of substrate to product

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7
Q

When a coenzyme is firmly associated with an enzyme, what is it known as?

A

A prosthetic group

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8
Q

Do many enzymes require cofactors for activity?

A

Yes

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9
Q

How are enzymes classified?

A

By the reaction they catalyse

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10
Q

What is the pH optimum for pepsin?

A

Acidic conditions

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11
Q

At what pH does carbonic anhydrase function optimally?

A

Neutral pH of plasma and cell cytoplasm

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12
Q

What is the optimum function condition for trypsin?

A

Alkaline conditions

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13
Q

In competitive inhibition, what happens to Km on the Lineweaver-Burke plot?

A

Km increases

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14
Q

What is methotrexate a structural analogue of?

A

Tetrahydrofolate

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15
Q

What enzyme does methotrexate specifically inhibit?

A

Dihydrofolate reductase

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16
Q

What is the effect of non-competitive inhibition on Vmax?

A

Vmax is decreased

17
Q

In non-competitive inhibition, what happens to Km?

A

Km is unchanged

18
Q

Where does the inhibitor bind in non-competitive inhibition?

A

At a site distinct from the active site

19
Q

What does cyanide inhibit?

A

Enzymatic activity (specifically, it can inhibit cytochrome c oxidase)