2.4 Enzymes Flashcards

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1
Q

What is the turnover number of an enzyme?

A

The number of reactions that an enzyme molecule can catalyse per second

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2
Q

What are intracellular enzymes?

A

Enzymes that catalyse reactions within a cell

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3
Q

What is an example of an intracellular enzyme?

A

Catalase , 4 polypeptide chains and an iron haem group found in small vesicles in eukaryotic cells used to kill invading microbes

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4
Q

What are extracellular enzymes?

A

Secreted enzymes out of cells to react with substrates extracellularly

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5
Q

What is an example of an extracellular enzyme?

A

Amylase in salivary glands to digest polysaccharide starch to maltose, it also made in the pancreas.

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6
Q

What is a permanently bound cofactor called?

A

A prosthetic group

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7
Q

What is an example of a prosthetic group?

A

carbonic anhydrase has zinc ion on its active site. This enzyme is found in erythrocytes (red blood cells).

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8
Q

What are non-permanently bound cofactors?

A

Cofactors that can bind to the substrate or to the enzyme to make forming bonds easier

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9
Q

What are non-protein molecules that bind permanently to the active site?

A

Coenzymes

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10
Q

Which cofactor is altered during reactions?

A

Coenzymes

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11
Q

What are some examples of vitamin coenzymes?

A

B12, floci acid, nicotinamide, pantothenate, thiamine

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12
Q

What are the 2 theories for enzyme-substrate complexes?

A

Induced fit, lock-and-key

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13
Q

What is the temperature coefficient?

A

The increase in rate of a process when the temperature increases by 10 degrees Celsius

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14
Q

What is the role of buffers in pH control?

A

Can accept or give hydrogen ions when needed to keep a desired pH

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15
Q

How are you doing today?

A

Daily affirmation: Ur cool

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16
Q

What are the 2 types of inhibitors?

A

Competitive Inhibitors that have a similar shape to the substrate and beat the substrate to the enzyme
Non-competitive inhibitors attach to other places other than the active site and disrupt the tertiary structure