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Biochemistry > Unit 5 - Redone > Flashcards

Unit 5 - Redone Flashcards

1
Q

Isoenzymes

A

Different forms of enzymes that catalyze the same reaction

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2
Q

How enzymes work

A

Increase rate of biochemical reactions that are already possible

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3
Q

What is acted upon by an enzyme?

A

Substrate

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4
Q

An enzyme increases the rate of a reaction how?

A

Lowering the activation energy needed

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5
Q

T/F: the ratio of the final equilibrium that already COULD occur between substrate and product are unchanged by an enzyme

A

True

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6
Q

Where are enzymes synthesized

A

Intracellularly

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7
Q

Where is ALKP produced?

A

BLIP
Bones, Liver, Intestines, Placenta

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8
Q

Do enzymes live/exist forever?

A

No, they eventually get degraded and metabolized out

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9
Q

Where do substrates bind?

A

To the active or catalytic site of an enzyme

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10
Q

What dictates which direction an enzymes occurs at?

A

Law of Mass Action
High to low concentration

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11
Q

What does an enzyme need to function?

A

Cofactor

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12
Q

Where do cofactors bind?

A

Allosteric site

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13
Q

Apoenzyme

A

Enzyme w/o cofactor

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14
Q

Holoenzyme

A

Enzyme w/ cofactor

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15
Q

Prosthetic group

A

Cofactor bound so tightly to the enzyme it looks like its part of the enzyme

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16
Q

Absolute specificity

A

Enzyme only reacts with one substrate

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17
Q

Group specificity

A

Enzyme only reactions with substrates that contain a specific group on the molecule

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18
Q

Stereoisomeric specificity

A

Enzymes only work with specific isomers or 3D configurations

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19
Q

Normally, what is supplied in excess to measure an enzymes activity?

A

Substrate

20
Q

First order kinetics

A

Low substrate concentration relative to excess enzyme concentration
Product formation depends on substrate concentration

21
Q

Zero order kinetics

A

Substrate in excess
Enzyme able to reach Vmax
Enzyme can’t work any faster

22
Q

Mixed order kinetics

A

Center of the graph that is mixed and unpredictable

23
Q

What does Km represent

A

Substrate concentration where enzyme catalyzes half as fast as it can (1/2 Vmax)

24
Q

How is the Km found?

A

Testing by Changing substrate concentration with a constant amount of enzyme present

25
Q

What should be in excess during enzyme measurement

A

Substrate

26
Q

What should be in excess during substrate measurement

A

Enzyme

27
Q

What does it mean if substrate exhaustion during enzyme measurement?

A

Loss of linearity in substrate measurement,
Dilute and retest

28
Q

High Km means

A

Low affinity

29
Q

Low Km means

A

High affinity

30
Q

The substrate with the highest Km will require…

A

The highest amount of substrate to achieve Vmax

31
Q

Lag Period

A

Little product formed

32
Q

Linear Period

A

Equilibrium reached
Vmax

33
Q

Nonlinear Period

A

Substrate exhaustion

34
Q

Standard International Unit of enzyme activity (IU/L)

A

Quantity of enzyme that will catalyze the reaction of 1 micromole of substrate/min

35
Q

First order kinetics linearity

A

0 to the Km

36
Q

Zero order kinetics linearity

A

Up to the Vmax

37
Q

Lineweaver-Burk plot X and Y axis

A

X - 1/Km
Y - 1/Vmax

38
Q

X intercept moves which way when Km is lower?

A

Left, enzyme activity is better

39
Q

X intercept moves which way when Km is higher?

A

Right, enzyme activity is worse

40
Q

Y intercept moves which way when the reaction slows down?

A

Up

41
Q

Y intercept moves which way when the reaction speeds up?

A

Down

42
Q

Km and Vmax with competitive inhibitions

A

Km increases
Vmax unaffected

43
Q

How does competitive inhibition work

A

Inhibitor binds to active site

44
Q

How does non competitive inhibition work

A

Inhibitor binds to allosteric site

45
Q

Non-competitive Inhibition Km and Vmax

A

Km unaffected
Vmax lower

46
Q

Uncompetitive Inhibition Vmax and Km

A

Km and Vmax both affected

47
Q

How does uncompetitive Inhibition work

A

Inhibitor binds Enzyme+Substrate complex

Biochemistry (26 decks)

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