Session 6 (Enzymes) Flashcards

1
Q

What is the transition state?

A

The high energy intermediate that lies between substrate and product

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2
Q

What bonding holds the enzyme substrate complex together?

A

Hydrogen, ionic, hydrophobic interactions

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3
Q

What is V0?

A

Initial rate of reaction

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4
Q

What is Km?

A

The [substrate] at which half of the enzymes are saturated (1/2 Vmax)

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5
Q

What is Vmax?

A

Max rate at which all enzyme active site are saturated

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6
Q

What shape is the graph that shows the relationship between [substrate] and enzyme saturation?

A

Retangular hyperbola

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7
Q

What does a high Km mean?

A

The enzyme has low affinity for substrate

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8
Q

What does a low Km mean?

A

The enzymes has a high affinity for the substrate

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9
Q

What is a unit?

A

The amount of enzyme that produces 1 um of products per min under standard conditions

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10
Q

How can a unit of enzyme be standardised?

A

By adding ‘per L of serum’ or ‘per g of tissue’ after it

Ie 2 units per L of serum

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11
Q

What other graph can be used to get values for Km and Vmax?

A

A double reciprocal

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12
Q

How do you read Km and Vmax values from a lineweaver Burk plot?

A

X intercept= -1/Km

Y intercept= 1/Vmax

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13
Q

When looking at a double reciprocal graph when is Km bigger?

A

The closer the x intercept gets to x=0

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14
Q

When looking at a double reciprocal graph, when is Vmax bigger?

A

When the y intercept is closer to y=0

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15
Q

How do enzymes work?

A

By lowering the Ea of a reaction

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16
Q

What affect do competitive inhibitors have on Km and Vmax?

A

Vmax-same

Km-reduced

17
Q

What affect do non-competitive inhibitors gave on Vmax and Km?

A

Vmax - decreases
Km- same
(No amount of substrate will enable full Vmax to be reached)