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BIOCHEM LEC > Function of Enzymes > Flashcards

Function of Enzymes Flashcards

1
Q

____ are proteins that speed up the rate of a chemical reaction in a living organism. Without enzymes, life as we know it would not exist.

A

Enzymes

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2
Q

An enzyme acts as a____ for specific chemical reactions, converting a specific set of reactants (called substrates) into specific products.

A

catalyst

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3
Q

Enzymes were named by adding the ____ to the name of the substrate. For example, urea (substrate) the enzyme is urease.

A

suffix “ase”

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4
Q

various chemical reactions occurring in a living organism

A

catalyzed

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5
Q

catalyze oxidation and reduction reactions in which electrons travel from one molecule to another

A

Oxido-reductases

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6
Q

Type of Reaction Of Oxido-reductases

A

oxidation and reduction

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7
Q

_____catalyze the transportation of a functional group from one molecule to another. Prime examples include aminotransferases, which catalyze amino acid degradation by removing amino groups.

A

Transferases

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8
Q

Two Type of Reaction of Transferases

A

Transamination and Phosphorylation

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9
Q

Transamination means

A

Transfer of amino group, the enzyme called transaminase

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10
Q

_____enzymes catalyze the hydrolysis of chemical bonds with the action of water (HOH)

A

Hydrolase

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11
Q

____ catalyze the breakdown of various chemical bonds by means other than hydrolysis and oxidation

A

Lyases

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12
Q

_____ is an example of a lyase that removes CO2 (carbon dioxide) from pyruvate.

A

Pyruvate decarboxylase

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13
Q

_____ catalyze structural shifts in molecules, causing changes in shape.

A

Isomerases

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14
Q

_____ catalyze ligation–the combination of pairs of substrates.

A

Ligases

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15
Q

For example,_____ is a ligase that catalyzes the interconversion of glucose and ATP with glucose-6-phosphate and ADP

A

hexokinase

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16
Q

ERASOIEMS

A

ISOMERASE

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17
Q

YLESSA

A

LYASES

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18
Q

ASSRRSEENTFA

A

TRANSFERASES

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19
Q

Two Theories of Enzyme Specificity

A

“lock and key” model and induced fit model

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20
Q

Model, proposed by____ in 1894

A

Emil Fischer

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21
Q

induced-fit model, which is a modification of the lock and key model that was proposed by ___ in 1958.

A

Daniel Koshland

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22
Q

enzyme and the substrate have three-dimensional shapes that fit each other

A

lock and key model

23
Q

proposes enzyme molecules that can change their shape, depending on the interaction with the substrate

A

induced-fit model

24
Q

What type of protein does enzyme?

A

Globular protein

25
Q

They range in size from ___ amino acids to more than 2,500 amino acid residues, but only a portion of their structure is involved in catalysis.

A

62

26
Q

The enzyme has what is called an ____, which contains one or more binding sites that orient the substrate in the correct configuration

A

active site

27
Q

part of the molecule that lowers the activation energy

A

catalytic site

28
Q

___ work by lowering the activation energy needed to make a chemical reaction occur

A

Enzymes

29
Q

Like other catalysts, enzymes change the ____of a reaction, but they aren’t consumed in the process. While most catalysts can act on a number of different types of reactions, a key feature of an enzyme is that it is specific. In other words, an enzyme that catalyzes one reaction won’t have any effect on a different reaction.

A

equilibrium

30
Q

Give 3 Factors Affecting Enzyme Activity

A

Effect of Temperature on Enzyme activity, Effect of pH on Enzyme Activity and Effect of Concentration

31
Q

TRUE/FALSE Low temperature increases the rate of enzyme activity because, at high temperatures, the substrate molecules move around faster so an enzyme is likely to come in contact with the substrate very quickly.

A

FALSE: high

32
Q

Most enzymes have 7-8 optimum pH, except for ____ where the optimum pH is 1.5 to pH 2.0.

A

pepsin

33
Q

Some enzymes require an additional chemical, called a___, for catalysis to occur.

A

cofactor

34
Q

TRUE/FALSE
-The cofactor could be a metal ion or an organic molecule, such as a vitamin. Cofactors may bind loosely or tightly to enzymes.

A

TRUE

35
Q

Tightly-bound cofactors are called _____

A

prosthetic groups.

36
Q

Give 3 examples of inorganic co-factors

A

ZINC, IRON & COPPER

37
Q

Give 2 examples of organic cofactors or coenzymes

A

MOST VITAMINS such as V. B2 and B5

38
Q

Poison Molecule

A

Alkaloid

39
Q

Example of Enzyme cofactor

A

Hemoglobin

40
Q

An enzyme made of __

A

Protein

41
Q

Where do substrates bind to an enzyme?

A

active site

42
Q

With what 3 letters do enzymes typically end

A

-ase

43
Q

What makes an enzyme substrate-specific?

A

Shape

44
Q

An enzyme speeds up a chemical reaction in the cell but can only be used once. True or False?

A

false

45
Q

What type of enzymes catalyze the transportation of a functional group from one molecule to another?

A

transferase

46
Q

The ____________model of enzyme action describes how an enzyme slightly changes its shape in order for a substrate to fit in better.

A

induced-fit

47
Q

_______inhibitors change the shape of an enzyme.

A

noncompetitive

48
Q

Enzymes are considered to be

A

Protein

49
Q

How do enzymes increase the speed of chemical reactions?

A

reducing the activation energy

50
Q

What is the name for the mechanism of enzyme activity?

A

Lock and key

51
Q

Which of the following is NOT true about enzymes?

A

Enzymes react with the substrate in a chemical reaction.

52
Q

Enzymes are composed of which of the following monomers?

A

amino acids

53
Q

What is the purpose of an enzyme?

A

speed up reactions

54
Q

Which of the following best explains why enzymes are necessary for many cellular reactions?

A

The reactions are too slow to meet the needs of the cell if enzymes are missing.

BIOCHEM LEC (6 decks)

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