Enzymes Flashcards

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1
Q

Enzyme-driven metabolic pathways can be made more efficient by

A
  • Concentrating enzymes within specific cellular compartments
  • Grouping enzymes into free-floating, multienzyme complexes
  • Fixing enzymes into membranes so that they are adjacent to each other
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2
Q

Common feature on all serine proteases is a:

A

Single reactive serine residue

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3
Q

Before they can react, many molecules need to be destabilized. This state is typically achieved through:

A

The input of a small amount of activation energy

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4
Q

What are serine proteases?

A
  • Chymotrypsin
  • Trypsin
  • Elastase
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5
Q

The catalytic activity of an enzyme is restricted to its small portion called:

A

Active site

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6
Q

An activated enzyme made of polypeptide chain and a co-factor is

A

Holoenzyme

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7
Q

An enzyme are sensitive to:

A

Changes in pH and changes in temperature

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8
Q

The “lock and key” model of enzyme action illustrates that a particular enzyme molecule

A

Interacts with a specific type of substrate molecule

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9
Q

Enzyme functions as

A

Organic catalyst

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10
Q

Many enzymes functions by ——- the activation energy of reactions

A

Lowering

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11
Q

An uncatalysed reaction requires a

A

Higher activation energy

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12
Q

The first step in any reaction catalysed by an enzyme is the formation of a specific association between the molecules called an

A

Enzyme-subrate complex.

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13
Q

The function of competitive inhibitors by their ability to interact or bind to

A

The active site of an enzyme

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14
Q

Which one inactivates an enzyme by indirectly changing the shape of the active site of an enzyme

A

Non-competitve inhibitor

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15
Q

What is a cofactor?

A
  • Inorganic ions
  • Organic molecules
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16
Q

What is a coenzyme?

A

Organic molecule

17
Q

When a molecule binds to an enzyme that is not the active site, and changes the shape of the enzyme so that is no longer can worl, this is called

A

Noncompetitve inhibition