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Chemistry > Enzymes > Flashcards

Enzymes Flashcards

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1
Q

What is a catalysis?

A

Study of how fast chemical reactions proceed

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2
Q

What is a catalyst?

A

A substance that increases the rate of chemical reactions

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3
Q

How do catalysts act?

A

By reducing the activation energy of a chemical reaction

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4
Q

What are enzymes?

A

Proteins which are biochemical catalysts

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5
Q

Relative specificity

A

Acting on several structurally related substances

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6
Q

Absolute specificity

A

Acting on one and only one substance

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7
Q

Stereochemical specificity

A

Acting on a specific stereoisomer

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8
Q

What can be regulated?

A

The catalytic behavior of an enzyme

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9
Q

What are coenzymes?

A

Organic molecules that act as cofactors

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10
Q

What are cofactors

A

Small organic molecules and ions (Zn, Co, Fe)

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11
Q

When can enzymes be catalytically active?

A

Only if a specific group or cofactors is attached to them

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12
Q

What makes an active enzyme?

A

Apoenzyme and cofactor (coenzyme or ion)

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13
Q

What is an active site?

A

Location on an enzyme where a substrate is bound to initiate catalysis

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14
Q

When does a binding of a substrate to the active site occur?

A

By matching intermolecular forces

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15
Q

What happens when an enzyme binds to a substrate?

A

Is forms an enzyme-substrate complex which releases a product

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16
Q

What is the lock-and-key model?

A

When the rigid enzyme and substrate have matching shapes.
Active site + substrate= EXACT FIT

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17
Q

What is the induced-fit model?

A

When the flexible enzyme changes shape to match the substrate.
Active site ADJUSTS to fit substrate

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18
Q

What is the enzyme activity?

A

The rate at which an enzyme catalyzes a reaction.
=speed

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19
Q

What is the turnover number?

A

The number of molecules of substrate acted on by one molecule of enzyme per minute.
=the amount

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20
Q

What factors affecting enzyme activity are due to kinetics ?

A

Enzyme and substrate concentration

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21
Q

What factors affecting enzyme activity are affecting the structure of an enzyme?

A

Temperature and pH

22
Q

Enzyme concentration

A

Increase the number of enzyme

23
Q

Substrate concentration

A

Increase substrate, reach max velocity

24
Q

What happens when you increase temperature?

A

denaturation

25
Q

What is an ezyme inhibitor?

A

A substance that decreases the rate of an enzyme-catalyzed reaction.

26
Q

What is an irreversible inhibition?

A

Forms. Strong bond with a specific functional group of an enzyme rendering it inactive.
(Kills enzymes)

27
Q

Reversible inhibition

A

Competitive and in competitive inhibitor

28
Q

Competitive inhibitor

A

Substrate + inhibitor takes the same spot in the enzyme.

29
Q

How to restore the activity of the enzyme?

A

By adding more substrate

30
Q

Noncompetitive inhibitor

A
  • Binds to the enzyme at a location other than the active site
  • cannot be reversed by adding more substrate
  • often changes the active site of the enzyme
31
Q

Activation of zymogens (proenzymes)

A

Inactive precursor of an enzyme

32
Q

Why are enzymes released in an inactive form?

A

To become fully active only when needed

33
Q

What happens when enzymes perform functions if they were released in an active form?

A

It could degrade cell components

34
Q

Allosteric regulation

A

Uses allosteric enzyme and modulator

35
Q

Allosteric enzyme

A

An enzyme whose activity is changed by the binding of modulators

36
Q

What is a modulator

A

A substance that binds to an enzyme at a location other than the active site and alters it’s catalytic activity.

37
Q

Example of Allosteric regulation

A

Final product becomes a noncompetitive inhibitor of an early enzyme in the pathway for biosynthesis of isoleucine.

38
Q

Genetic control

A

The synthesis of proteins is under genetic control

39
Q

Example of genetic control

A

Enzyme induction : synthesis of enzymes in response to a temporary need of the cell

40
Q

When cells are damaged or die, what do enzymes do?

A

Reside inside the cells and are released

41
Q

How to detect a condition in the concentration of enzymes in blood?

A

If level goes up. Usually, the level remains low

42
Q

Isoenzymes

A

Slightly different form of the same enzyme produced by different tissues (ex: LDH)

43
Q

What is used in the diagnosis of a wide range of diseases!

A

Serum levels of LDH due to the difference in tissue distribution of LDH isoenzymes.

44
Q

Alkaline phosphate (ALP)

A

Liver or bone disease

45
Q

Amylase

A

Pancreas disease

46
Q

Creatinine phosphokinase

A

Heart attack

47
Q

Aspartate transaminase (AST)

A

Liver and/or heart attack

48
Q

Alanine transaminase (ALT)

A

Hepatitis

49
Q

Lactate dehydrogenase (LDH) l

A

Liver and/or heart attack

50
Q

Lipase

A

Acute pancreatitis

51
Q

Lysozyme

A

Monocytic leukemia

Chemistry (10 decks)

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