UNIT#07 ENZYMES Flashcards

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1
Q

If enzymes stop their functions, then biochemical reactions would:

A

Be slowed downs

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2
Q

All of the following are true or an enzyme except:

A

Increase the energy of activation

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3
Q

Enzymes catalyze all of the following except:

A

Breathing

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4
Q

The lower the activation energy, the ____ the reaction will be:

A

Faster

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5
Q

Most of the enzymes are:

A

Attached wiht organelees

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6
Q

Enzymes related to fatty acids oxidation are present in/at:

A

Mitochondria
(Fatty acid metabolism)

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7
Q

Al enzymes are ____.

A

Globular proteins

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8
Q

The reactants on which enzymes work are:

A

Substrates

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9
Q

What is true about enzymes?

A

No effect on the end product

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10
Q

The main difference between catalysts and enzymes is:

A

Catalysts are inorganic while enzymes are organic in nature

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11
Q

The type of energy reduced by the enzymes for biological reactions to occur is called the:

A

Activation energy

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12
Q

It is false about enzymes:

A

➡All enzymes require a co-factor for proper functioning✅
➡Only a small amount of enzymes is required❌
➡THey work in vitro as well as in vivo conditions❌
➡They lower activation energy❌

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13
Q

Biochemically enzymes are:
(all enzymes are globular)

A

Proteins

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14
Q

All enzymes are proteins:

A

Globular

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15
Q

Three-dimensional globular protein is:

A

Enzymes

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16
Q

Which of the following is NOT a globular protein?

A

Increases the rate of reaction

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17
Q

Enzymes involved in cellular respiration are found in:

A

Mitochondria

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18
Q

Which of the following is an example/s of enzymes attached to membrane systems inside the cell in a specific and orderly arrangement?

A

➡Mitochondira
➡Chloroplast

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19
Q

The reaction will proceed faster if the activation energy is?

A

Low

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20
Q

The energy required to start a reaction is called?

A

Activation energy

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21
Q

An enzyme that requires a biological change in order to become active is called?

A

Zymogen

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22
Q

AN enzyme without its cofactor is called:

A

Apoenzyme

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23
Q

If the non-protein part of the enzyme is covalently bonded to the enzyme it is known as?

A

Prosthetic group

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24
Q

Small organic, the non-protein part that helps in enzyme reactions:

A

Co-factor

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25
Q

An activated enzyme made up of a polypeptide with its cofactor is:

A

Holoenzyme

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26
Q

Nicotinamide adenine dinucleotide is an example of:

A

Co-enzyme

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27
Q

Co-enzyme requires:

A

Vitamins

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28
Q

Which of the following form weak linkage with an enzyme?

A

Co-enzyme

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29
Q

Co-factors are divided into groups:

A

3

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30
Q

The substrate binds to a specific region of an enzyme called?

A

Active site

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31
Q

All enzymes are:

A

Globular proteins

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32
Q

What does the active site of the enzyme determine?

A

Determines by its structure the specificity of an enzyme

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33
Q

Enzymes showing substrate specificity are specific to how many substrates?

A

1

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34
Q

Which term is used to refer to an inactive enzyme precursor?

A

Zymogen

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35
Q

Catalysts that increase the rate of biological chemical reactions are called?

A

Enzymes

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36
Q

Which of the following best describes a co-enzyme?

A

Loosely bonded non-protein part of an enzyme

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37
Q

Which statement about enzymes is incorrect?

A

➡Some of them consist solely o protein with no non-protein part❌
➡They catalyze a chemical reaction without being utilized❌
➡They without their cofactor are called apoenzyme❌
➡All enzymes are fibrous proteins ✅

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38
Q

The active form of an enzyme:

A

holoenzyme

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39
Q

A cofactor made of inorganic on which is detachable is called

A

Activator

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40
Q

Enzymes are globular proteins because

A

They have a tertiary structure

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41
Q

A small organic, non-protein molecule that carries chemical groups between enzymes are:

A

Co-enzyme

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42
Q

Biological molecules which catalyze a biochemical reaction and remain unchanged after completion of the reaction are called:

A

Enzymes

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43
Q

Enzymes bind with chemical reactants known as:

A

Substrate

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44
Q

Which of the following vitamin acts as a coenzyme

A

➡Vitamin B
➡Vitamin B2

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45
Q

If the non-protein part of the enzyme is covalently bonded to the enzyme it is known as?

A

Prosthetic group

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46
Q

The enzyme reacts with the substrate to form:

A

Product

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47
Q

Enzymes are ____ in nature:

A

Proteins

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48
Q

Which type of bond is never formed when the substrate fits into the active site of the enzyme

A

Hydrophobic interaction

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49
Q

The mechanism of enzyme activation is referred to as:

A

Catalysis

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50
Q

The specificity of enzyme structure depends upon:

A

Active site

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51
Q

The catalytic activity takes place at:

A

Active site

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52
Q

Which statement about the active sites is not true?

A

➡Acitve site is a spherical shape❌
➡Active site is non-specific✅
➡Active site contains few amino acids❌
➡Active site converts the substrate into product❌

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53
Q

Type of bond present between enzyme and prosthetic group:

A

Covalent

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54
Q

Which one forms the raw material for coenzymes?

A

Vitamins

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55
Q

The reaction takes place in a small part of the enzyme is called:

A

Active site

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56
Q

Coenzymes are closely related to;

A

Vitamins

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57
Q

The atoms, groups of atoms and molecules that join with enzymes that alter their shape and make them functional

A

Co-factors

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58
Q

If the cofactor is a non-protein like a metallic ion, it is referred to as a:

A

Activator
(Metallic ion)

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59
Q

The non-protein part which is organic in nature and detachable is called:

A

Coenzyme

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60
Q

The function of succinate dehydrogenase is aided by:

A

FAD+

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61
Q

Prosthetic groups are:

A

Organic molecules

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62
Q

All coenzymes are derived from:

A

Vitamins

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63
Q

A co-factor tightly bound to the enzyme on a permanent basis is called:

A

Prosthetic Group

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64
Q

An enzyme is required Mg+2 to catalyze the substrate. The Mg+2 is the best identified as:

A

Activator

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65
Q

Which of the following comprises inorganic ions?

A

Activators

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66
Q

A non-protein part essential for the proper functioning of the enzyme is called:

A

Co-factor

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67
Q

An enzyme that is non-protein in nature:

A

Peptidyl transferase
➡Ribozyme(made up of RNA)

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68
Q

An enzyme and substrate react through definite charge-bearing sites.

A

Active site

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69
Q

The active site of an enzyme:

A

Determine by its structure, the specificity of the enzyme

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70
Q

The specificity of the enzyme is due to its _____.

A

Configuration

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71
Q

The lock and key model was proposed by:

A

Emil Fischer

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72
Q

According to the Lock and Key model, the active site is:

A

Rigid structure

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73
Q

The lock and key model of enzyme action were proposed by:

A

Emil Fischer

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74
Q

The complex that forms when a substrate binds to the enzyme is called;

A

Enzyme-substrate complex

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75
Q

Who proposed the lock and key model of enzyme activity?

A

Emil Fischer

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76
Q

In the lock and key model of enzyme activity, the substrate acts as the;

A

Lock

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77
Q

Do enzymes work by which of the following?

A

Reducing the activation energy

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78
Q

How many models are present for enzyme-substrate complex or reaction?

A

2

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79
Q

Which statement is incorrect about the lock and key model?

A

➡Specific enzyme can transform only a specific substrate❌
➡Ative site of an enzyme is a non-flexible structure❌
➡Active site does not change before during or even after reaction❌
➡It explains the mechanism of every chemical reaction✅

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80
Q

Which types are never formed when a substrate fits into the active site of an enzyme?

A

Covalent linkages

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81
Q

Koshland in 1959 proposed the modified form of which the following?

A

Induced fit model

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82
Q

The induced fit model was introduced by Koshland in which of the following year?

A

1959

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83
Q

The lock and key model was proposed by:

A

Fischer

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84
Q

Which of the following is false concerning enzymes?

A

Enzymes increase both the forward rate and reverse rate of a reaction

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85
Q

A number of substrate molecules converted into the product by one molecule of enzyme active site per unit time is called:

A

Turnover number

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86
Q

According to the induced fit model, what happens when an enzyme-substrate complex is formed?

A

The contact between the substrate and the enzyme causes a change in the shape of the active site

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87
Q

What effect do enzymes have on the activation energy of a reaction?

A

Decrease

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88
Q

While bound to the active site, the substrate is converted into which of the following?

A

Product of reaction

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89
Q

The primary function of co-factors is to?

A

Assist in enzyme activity

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90
Q

In enzyme catalytic reaction the substrate is first converted to a high energy state called?

A

Transition state

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91
Q

Allosteric enzymes consist of multiple:

A

Polypeptide chains

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92
Q

The function of enzymes includes all of the following:

A

Shifting substrates into more favourable positions in the active site

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93
Q

ES complex is converted into the product by:

A

Catalytic site

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94
Q

____ suggested that each enzyme had a particular shape into which the substrate fits exactly.

A

Amil Fischer

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95
Q

Allosteric enzymes have ____ major sites.

A

2

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96
Q

According to the ____ model, the active site of the enzyme is modified as the substrate interacts with the enzyme.

A

Induced fit model

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97
Q

A modified form of the Lock and model was proposed by:

A

Koshland

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98
Q

According to Lock and Key model, the enzymes acts as:

A

Key

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99
Q

The working of sucrase and maltase can be explained by:

A

Lock and Key Model

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100
Q

With the increase of enzyme concentration in a reaction, more ____ is/are available for the substrate.

A

Binding sites

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101
Q

The lock and key model for enzyme action proposed by Emil Fischer suggest that:

A

Enzymes are restricted to one reaction type

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102
Q

The effect of a reversible competitive inhibitor can be neutralized by increasing the concentration of:

A

Substrate

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103
Q

If the concentration of the substrate molecule is higher than the enzymes then the rate of reaction would be:

A

Remain constant

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104
Q

Optimum pH of enterokinase is:

A

Slightly acidic
(pH= 5.50)

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105
Q

Which of the following properties of amino acids is affected by a change in pH?

A

Ionization of amino acids

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106
Q

Change in tempertue from 30C to 40 C in human body will cause:

A

First increase then decreases the rate of reaction

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107
Q

Which of the following factor does not affect the rate of enzyme acton?

A

Light intensity

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108
Q

Which one of the following is the optimum pH of pancreatic lipase enzyme?

A

➡7.60=Catalase
➡9.00=Pancreatic Lipase
➡8.00=Chymotrypsin
➡9.70=Arginase

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109
Q

The temperature that promotes the maximum activity of enzyme is referred as:

A

Optimum Temperature

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110
Q

Which type of bond is mostly affected in an enzyme molecule when there is pH fluctuation?

A

Ionic Bonds

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111
Q

Most enzymes have an optimum temperature of around:

A

40C

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112
Q

Enzymes which require optimum temperature to be lower than 37C for their proper functioning are present in:

A

Testes
(Spermatogenesis takes place at 35C)

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113
Q

Which of the following statement is correct?

A

All enzymes in human body work at same temperature but different pH

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114
Q

Bond sensitive to change in temperatre and pH are respectively:

A

➡Hydrogen (Temperature)
➡Ionic (pH)

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115
Q

The tempeature where inactive enzyme becomes active is called:

A

Minimum Temperature

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116
Q

The rate of an enzyme-controlled reaction increases rapidly if the amount of enzyme is doubled in the presence of an unlimited substrate concentration. This is due to:

A

Number of active sites increase

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117
Q

THe optimum tempearture for enzymes to work at maximum rate in human is:

A

37C

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118
Q

Enzymes lower down the energy of:

A

Activation

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119
Q

Optimum pH for pepsin is:

A

2.00

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120
Q

4.50 is the optimum pH value for the enzyme:

A

Sucrase

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121
Q

Optimum pH for sucrase is:

A

4.50

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122
Q

Optimum pH for enterokinase enzyme is:

A

5.50

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123
Q

Salivary amylase acts best at pH:

A

6.8

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124
Q

The enzyme with optimum pH=7.60 is;

A

Catalase

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125
Q

The optimium pH of pancreatic lipase is:

A

9.0

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126
Q

The optimum pH for enzyme arginase is:

A

9.70

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127
Q

A little change in pH may lead to:

A

Ionization of active site of an enzyme

128
Q

Extreme changes in pH cause the bonds in the enzyme to break, resulting in the enzyme:

A

Denaturation

129
Q

Upon increasing the temperature the shape of enzyme’s active site?

A

Denatures

130
Q

The optimum pH for enzyme arginase is which of the following?

A

9.7

131
Q

The optimum pH for the function of the enzyme pepsin is?

A

2

132
Q

If we add more substrate to an already occurring enzymatic reaction and it has no effect on the rate of reaction, the process is called?

A

Saturation

133
Q

pH of salivary amylase is:

A

6.8

134
Q

It works in acidic medium

A

Enterokinase

135
Q

Extreme chagne in pH results in which of the following?

A

Denaturation of the enzyme

136
Q

What is meant by optimum temperature of an enzyme?

A

The tempertature at which an enzyme makes the maximum amount of product

137
Q

Rate of reaction is double for rise of every _____.

A

10C

138
Q

Which of the following strategies of enzymatic inhibition is used by noncompetitive inhibitors?

A

Bind to an allosteric site to cause a conformational shift in the enzyme

139
Q

If more substrate to an already occuring enzymatic reaction is added more enzyme activity is seen because:

A

There is probably more substrate present than there is an enzyme

140
Q

The optimum pH for the functioning of pancreatic lipase is?

A

9

141
Q

A researcher has designed a new type of inhibitor that binds at the active site of an enzyme. What type of inhibition does this molecule display?

A

Competitive inhibition

142
Q

Which of the following changes could lead to loss of enzymatic function?

A

Increase in pH of the reaction

143
Q

Which statement correctly describes why enzyme activity increases with increased enzyme concentration?

A

Collisions between enzyme and substrate molecules because more active sites are available

144
Q

The rate of reaction enzyme directly depends upon which of the following?

A

Amount of enzyme present at a specific time at an unlimited substrate concentration

145
Q

The enzyme-substrate complex is formed in which part of the enzyme molecule?

A

Binding site

146
Q

Which step, causes activation of the catalytic site of an enzyme?

A

Formation of enzyme-substrate site

147
Q

If the concentration of enzyme is kept constant and the amount of substrate is increased a point is reached where an increase in substrates concentration does not affect the reaction rate because of:

A

All the active sites on the enzyme molecule are occupied

148
Q

What is the optimum temperature for working enzymes in the human body?

A

37C

149
Q

In an acidic medium, amino acids carry a positive charge and act as:

A

Base

150
Q

If we increase the pH then, enzyme reactivity is retarded due to:

A

The tertiary structure of the enzyme is destroyed

151
Q

When we increase the concentration of substrate then an increase in the enzyme activity is due to which of the following?

A

It is a sufficient concentration of enzyme

152
Q

At low enzyme concentration, optimum pH and temperature, the rate of reaction can be increased by:

A

Increasing enzyme concentration

153
Q

The number of substrate molecules converted into the product by one molecule of enzyme active site per unit is called

A

Turn over number

154
Q

The competitive inhibitors have structural similarities with:

A

Substrate

155
Q

Which of the following type of inhibitor can be neutralized by adding more substrate into the reaction?

A

Reversible inhibitor

156
Q

If a molecule can bind to another site of the enzyme rather than the true active site, it is referred to as:

A

Non-Competitive inhibitors

157
Q

What is common in both competitive and non-competitive inhibition?

A

Reversible inhibition

158
Q

A student of chemical engineering mistakenly engulfed the toxic compound “A” which was a potent inhibitor of certain enzymes. He was immediately brought to the hospital where the doctor injected intravenously substrate “B” to minimize the toxic effect of compound A. His life was saved from serious damage. The treatment method shows that compound A was a ____ inhibitor.

A

Competitive Reversible

159
Q

Penicillin, an antibiotic inhibits bacterial growth. It is characterized as:

A

Irreversible inhibitors

160
Q

Which of the following is not an inhibitor of enzymes?

A

Sucrose

161
Q

Heavy metal ions that act as inhibitors (mercury, silver and copper) break ____ in enzymes.

A

Disulphide bridges

162
Q

Poisons like cyanide, antibiotics and some drugs are examples of:

A

Inhibitors

163
Q

The inhibitors that bind tightly and permanently to enzymes and destroy their globular structure stopping their catalytic activity are:

A

Irreversible inhibitors

164
Q

The type of inhibition in which the inhibitor has no structural similarity to the substrate and combines with the enzyme at other than the active site is called:

A

➡Non-competitive
➡Reversible inhibition

165
Q

Enzyme succinate dehydrogenase converts succinate into:

A

Fumarate

166
Q

The effect of a competitive inhibitor on enzyme activity is such that it affects which of the following?

A

Decreases enzyme activity

167
Q

What is the characteristic of a non-competitive inhibitor?

A

Adding more substrate does not reduce the effects of inhibition

168
Q

Do reversible inhibitors form weak linkages with which of the following?

A

Enzyme

169
Q

Inhibitors which block the enzyme by forming weak bonds are called:

A

Competitive inhibitors

170
Q

Do reversible inhibitors form weak linkages with which of the following?

A

Enzyme

171
Q

The end product of an enzymatic reaction inhibits the formation of the product in an earlier step. This type of enzymatic regulation is known as:

A

Feedback Inhibition

172
Q

In incompetitive inhibition, the inhibitor binds with:

A

Enzyme

173
Q

In mixed inhibition, the allosteric effects:

A

Shape of enzyme

174
Q

The non-substrate molecules that bond to the allosteric sites are called?

A

Inhibitors

175
Q

A chemical substance which can react (in place of the substrate) with the enzyme but is not transformed into a product/s and thus blocks the active site temporarily or permanently is called?

A

Inhibitor

176
Q

Malonic acid is an example of which type of inhibitor.

A

Competitive Inhibitors

177
Q

In non-competitive inhibition, the quantity which remains the same as the reaction proceeds are?

A

Km

178
Q

A substrate which binds at the active site of the enzyme but does not result in the formation of the products is called:

A

Competitive inhibitor

179
Q

An inhibitor is added, disrupting the function of a particular enzyme. The experimenter adds more substrate, and enzyme function increases again. These results indicate the involvement of what type of inhibitor?

A

Competitive

180
Q

What is meant by enzyme denaturation?

A

➡Peptide bonds between amino acid residues are broken
➡The enzyme loses its secondary structure
➡The enzyme loses its tertiary structure
✅All of the above

181
Q

The effect of a competitive inhibitor on enzyme activity is such that it affects which of the following?

A

Decreases enzyme activity

182
Q

The non-substrate molecules that bind to the allosteric sites are called?

A

Inhibitors

183
Q

Which of the following best describes competitive inhibitors?

A

Resemble structurally with the substrate

184
Q

____ is a competitive inhibitor of succinic dehydrogenase.

A

Malonic acid

185
Q

In competitive inhibition, a thing that binds to the enzyme active site is?

A

Inhibitors

186
Q

Feedback inhibition in most metabolic pathways involves which type of enzymes?

A

Allosteric enzymes

187
Q

These form weak linkages with enzymes:

A

Reversible inhibition

188
Q

In uncompetitive inhibition, the inhibitor bonds with:

A

ES Complex

189
Q

An allosteric enzyme will have:

A

Many binding sites

190
Q

In mixed inhibition, the inhibitor binds to:

A

Allosteric site

191
Q

Competitive inhibitors ____ enzyme activity.

A

Decrease

192
Q

The structure of the enzyme is altered by:

A

Non-Competitive inhibitor

193
Q

In competitive inhibition, two things attached to the enzyme’s active site are:

A

Substrate

194
Q

The structure of an enzyme is altered by which of the following inhibition?

A

Irreversible inhibitor

195
Q

Do phosphatases belong to which group of the following?

A

Hydrolases

196
Q

Cytochrome oxidase is categorized in:

A

Oxidoreductases

197
Q

Conversion of glucose 6-phosphate into fructose 6-phosphate is done by:

A

Isomerases

198
Q

A statement that is not correct about enzymes;

A

➡They increase the rate of reaction❌
➡They contaminate end product✅
➡They lower the activation energy❌
➡They cannot start chemical reactions❌

199
Q

When apoenzyme is separated from its metal compoenent, its activity is:

A

Lost

200
Q

Synthesis of enzymes takes place by:

A

Translation

201
Q

This is the core of induce fit model which distinguishes it from lock and key model

A

Change in enzyme

202
Q

Which of the following is common between Lock and Key model and Induce Fit model?

A

Enzymes are specific in nature

203
Q

Extreme changes in pH cause denaturation of enzyme by breakign:

A

Ionic bond

204
Q

After a certain limiting concentraion of substrate, increasing the concentration of enzyme two times, rate of reaction will:

A

Remain constant

205
Q

Their effect can be neutralized completely or partly by an increase in the concentration of substrate;

A

Reversible competitive

206
Q

In an enzyme controlled chain reaction, if concentration of initial substrate is increased then it will cause:

A

Precursor activation

207
Q

The enzyme needed in biological systems for joining two molecuels is called;

A

Ligases

208
Q

Cofactors are;

A

➡Prosthetic groups
➡metallic ions
➡Co-enzymes

209
Q

In eukaryotes, enzymes are mostly

A

Bound to organelles

210
Q

Synthesis of enzymes takes place by;

A

Translation

211
Q

The catalytic activity of an enzyme is restricted to a small portion of the structure known as:

A

Active site

212
Q

An enzyme and its substrate react with each other through a definite charge bearing site called;

A

Active site of enzyme

213
Q

If any factor alters the chemistry and configuration of an enzyme, it will probably be:

A

➡Temperature
➡pH
➡Inhibitor

214
Q

The rate of reacton depends directly on the amount of enzyme present at a specific time at;

A

Unlimited substrate concentration

215
Q

Their effect can be neutralized completely or partly by an increase the concentration of substrate;

A

Reversible competitive

216
Q

In Krebs cycle, malonic acid blocks succinic dehydrogenase thorugh;

A

Reversible competitive inhibition

217
Q

They occupy the active sites by forming covalent bonds;

A

Irreversible inhibitors

218
Q

Any agent which reduces/slows down or stops the rate of reacton of enzymes is termed as

A

Inhibitor

219
Q

In an enzyme controlled chain reaction, if concentraion of initial substrate is increase then it will cause;

A

Precurosr activation

220
Q

In feedback inhibition, a metabolic pathway is switched off by:

A

Accumulation of end product

221
Q

Amylase is an example of ;

A

Hydrolase

222
Q

The enzymes catalyzing re-arrangement of atomic grouping without altering molceular weight or number of atom is;

A

Isomerases

223
Q

The enzyme needed in biological systems or joining two molecules is called:

A

Ligases

224
Q

Which of the following is more specific?

A

➡Lactase✅
➡Pepsin❌
➡Trypsin❌
➡Lipase❌

225
Q

Which of the following is an example of a coenzyme?

A

FAD+ in Krebs cycle during succinate conversion to fumarate

226
Q

The optimum pH for working of pancreatic lipase is:

A

9.00

227
Q

Phosphorylation of glucose is done by:

A

Kinase

228
Q

An enzyme which catalyzes different substrates into single product:

A

Hexokinase

229
Q

ATP binds to ____ of phosphofructokinase:

A

Allosteric site

230
Q

The temperature where an inactive enzyme becomes active again is called:

A

Minimum Temperature

231
Q

Changing the pH from optimum results in:

A

Decrease in rate of reaction

232
Q

Which of the followings is not an inhibitor of enzymes?

A

Maltose

233
Q

Which enzyme can digest the following molecule?

A

➡Amylase❌
➡Pepsin❌
➡Lipase✅
➡Lactase❌

234
Q

A protein that is not an enzyme:

A

➡Isomerase❌
➡Rennin❌
➡Prolactin✅
➡Maltase❌

235
Q

The active site of an enzyme:

A

Determines by its structure the specificity fo the enzyme

236
Q

Which of the following is the features of the enzymes:

A

➡Non-Crystalline❌
➡Spindle Shape❌
➡Soluble in aqueous medium✅
➡Fibrous Shape❌

237
Q

The essential chemical components of many coenzymes are:

A

Vitamins

238
Q

Select the option which is not correct with respect to enzyme action:

A

➡The addition of succinate does not reverse the effect produced by malonate✅
➡Malonate is a competitive inhibitor o succinate dehydrogenase❌

239
Q

The specificity of enzyme was first proposed by:

A

E. Fischer

240
Q

The temperature, where an inactive enzyme becomes active again, is called:

A

Minimum Temperature

241
Q

All enzymes follow the induced fit model except:

A

➡Carbonic anhydrase❌
➡Allosteric Enzymes❌
➡Hexokinase❌
➡Urease✅

242
Q

Cyanides are potent poisons for the living organisms because they can kill by inhibiting ____, essential for cellular respiration.

A

Cytochrome Oxidase

243
Q

Penicillin control bacterial infection by:

A

Reversible Non-Competitive

244
Q

Which one of the following is called biological catalysts?

A

Enzymes

245
Q

The active site of enzymes consists of:

A

Only a few amino acids

246
Q

_______ maintains the globular structure of the enzyme

A

The bulk of amino acids

247
Q

Often it contributes directly to the chemical reactions which bring about catalysis:

A

Co-Factor

248
Q

If the non-protein part of the enzyme is covalently bonded to the protein part, it is called

A

Co-Enzyme

249
Q

An activated enzyme consisting of polypeptide chain and a cofactor is known as:

A

Holoenzyme

250
Q

Enzymes are sensitive to even a minor change in:

A

➡pH
➡Temperature
➡Substrate COncentration

251
Q

________ is a powerful protein digesting enzyme and is capable of destroying a cell’s internal structure and thus produced in inactive ________ form by the cell

A

Pepsin, Pepsinogen

252
Q

After the formation of products, it is released unaltered and thus can be used again:

A

Enzyme

253
Q

Enzymes involved in some metabolic pathways are normally present together:

A

In precise order

254
Q

The charge and shape of the active site of the enzyme is formed by _______ in the polypeptide chain of the active site of the enzyme.

A

Some amino acids

255
Q

The reaction between _______ activates the catalytic site of the enzyme

A

Substrate and Binding site of the enzyme

256
Q

According to this model enzyme is a rigid structure:

A

Lock and Key Model

257
Q

According to ________ the active site of enzyme is not a rigid structure

A

Induced Fit Model

258
Q

The functional specificity of every enzyme is the consequence of its:

A

Specific chemistry and Cofiguration

259
Q

The rate of reaction depends directly on the amount of enzyme provided the substrate concentration is

A

Unlimited

260
Q

By increasing the enzyme molecules ________ will convert the substrate molecules into products, in the given period of time.

A

More active sites

261
Q

If the enzyme conc. is kept constant, by increasing the substrate concentration the rate of enzyme action is

A

Increased or specific time

262
Q

The rate of enzyme-controlled reactions may increase with the increase in:

A

Temperature up to optimum level

263
Q

Chemical reactions are accelerated at high temperature because

A

Heat provides the activation energy

264
Q

When reactants move more quickly and chances of their collision with each other are increased as a result the rate of enzyme-controlled reactions will?

A

Increase Initially

265
Q

Inhibitors can be divided into:

A

Two basic types

266
Q

They alter the structure of the enzyme in such a way that even if genuine substrate binds the active site, catalysis fails to take place temporarily:

A

Non-Competitive Inhibitors

267
Q

Pick up the product:

A

➡Succinic Acid❌
➡Malonic Acid❌
➡Fumaric Acid✅
➡Dehydrogense❌

268
Q

Succinic acid dehydrogenase + malonic acid ➡

A

No reaction possible, Enzyme is blocked

269
Q

Which one of the following is reused?

A

Enzyme and Co-enzyme

270
Q

Some enzymes are potentially damaging if they are manufactured in their active form e.g.

A

Pepsin

271
Q

Which one of the following products will
control this pathway through feedback
activation?
A➡B➡C➡D➡E

A

E

272
Q

Which one of the following products will control this pathway through feedback action
A➡B➡C➡D

A

E

273
Q

A➡B➡C➡D➡E
Accumulation of “E” will control the above pathway through:

A

Feedback Inhibition

274
Q

A➡B➡C➡D➡E
A deficiency of “E” will control the above
pathway through:

A

Feedback activation

275
Q

Induce fit model was proposed by

A

Koshland

276
Q

Salivary amylase works best at pH:

A

6.80

277
Q

Optimum pH for the action of pancreatic lipase is:

A

9.00

278
Q

Malonic acid is competitive inhibitor of:

A

Succinic Dehydrogenase

279
Q

It causes denaturation of globular structure of enzyme:

A

Extreme pH change

280
Q

Any molecule that increases the rate of a chemical reaction without being used up during that reaction is called:

A

Catalyst

281
Q

Enzymes are not synthesized in:

A

Viruses

282
Q

Enzymes enhance the rate of reaction by:

A

Lowering the activaton energy of the reaction

283
Q

Which enzyme hydrolyses internal phosphodiester bonds in a polynucleotide chain?

A

Endonuclease

284
Q

Which one of the following statements regarding enzyme inhibition is correct?

A

Competitive inhibition is seen when substrate and inhibitor compete

285
Q

A competitive inhibitor of succinic dehydrogenase is:

A

Malonic acid

286
Q

Enzymes often have additional parts in their structures that are made up of molecules other than proteins. When this additional chemical part is an organic molecule, it is called:

A

Co-Enzyme

287
Q

The lipid synthesizing enzymes are present in:

A

Smooth ER

288
Q

The term apoenzyme is applicable to:

A

Protein part of conjugate enzyme

289
Q

Enzymes:

A
290
Q

Enzymes generally have:

A

Different pH but same optimum temperature

291
Q

Koshland’s model of enzyme action is known as:

A

Induced Fit model

292
Q

Enzymes having slightly different molecular structure but performing identical activity are:

A

Isoenzymes

293
Q

Which factor is responsible for the inhibition enzymatic process during feedback

A

End Product

294
Q

One which is not an inhibitor:

A

Metabolites

295
Q

Some of the enzymes, which are associated with converting fats into carbohydrates, are present in:

A

Glyoxysomes

296
Q

Any molecule which acts directly on an enzyme to lower its catalytic rate is called:

A

Inhibitor

297
Q

Which of the following statements is true regarding enzyme inhibition?

A

➡It may be reversible or irreversible
➡Reversible can be competitive or noncompetitive

298
Q

The effect of a reversible competitive inhibitor can be nullified by:

A

Increasing the substrate concentration

299
Q

The ____ acts as a “bridge” between the enzyme and its substrate.

A

Co-Factor

300
Q

One which is inorganic in nature:

A

Activator

301
Q

The following is a substrate-specific enzyme:

A

➡Pepsin❌
➡Protease❌
➡Lipase❌
➡Sucrase✅

302
Q

Regarding the nature of enzymes, which one is correct?

A

They are specific both in their nature and action

303
Q

Regarding enzyme molecules:

A

Greater in size than the substrate

304
Q

The temperature at which enzymes can work at their maximum rate is called ____ temperature.

A

Optimum

305
Q

The optimum pH for enterokinase is:

A

5.50

306
Q

Which of the following does not work on an acidic medium:

A

Arginase

307
Q

An enzyme and substrate react through a special feature or site present in an enzyme known as:

A

Active Site

308
Q

Enzymes increase the rate of reaction by:

A

Decreasing activation energy

309
Q

The non-protein part of enzyme which is covalently bonded is called:

A

Prosthetic Group

310
Q

Most vitamins are

A

Co-Enzymes

311
Q

Which of the following is a co-factor?

A

➡Calcium Ions
➡Copper Ions
➡Manganese ions

312
Q

Co-Enzymes combine with:

A

Apoenzyme

313
Q

The non-competitive inhibitor is one that:

A

Binds away from the active site of an enzyme

314
Q

The shape of enzyme molecule is:

A

Globular

315
Q

The protein cytochrome c functions only when it contains an atom of iron. Which term describes the atom of iron?

A

Part of a prosthetic group