Enzymes/N-metabolism Years 2013-2009

Question

The Michaelis-Menton model:

Answer 1

Is based on the assumption that a transition state is formed in the enzyme active site.

Answer 2

Is based on the assumption that an enzyme catalysed reaction is mediated at the active site of an enzyme.

Answer 3

Is based on the assumption that a biochemical reaction is at equilibrium.

Answer 4

Is based on the assumption that a biochemical reaction occurs at a steady state.

Answer 5

Is associated with the maximum enzyme activity observed when the all active sites in an enzyme are saturated with substrate.

Answer 6

Is associated with the number of substrate molecules reacted on by an enzyme molecule per unit time.

Answer 7

Is associated with the affinity of an enzyme for a specific substrate.

Answer 8

Is associated with the selectivity of an enzyme for different substrates.

Answer 9

Is a measure of the rate of acceleration carried out by the enzyme.

Answer 10

For a given enzyme is independent of the substrate used.

Answer 11

Has units of concentration.

Answer 12

Gives an idea of the enzymes catalytic efficiency.

Answer 13

Is associated with the maximum enzyme activity observed when the all active sites in an enzyme are saturated with substrate.

Answer 14

Is associated with the number of substrate molecules reacted on by an enzyme molecule per unit time.

Answer 15

Is associated with the affinity of an enzyme for a specific substrate.

Answer 16

Is associated with the selectivity of an enzyme for different substrates.

Answer 17

A catalytic strategy facilitating transition state formation through covalent bond formation between the substrate and enzyme active site.

Answer 18

A catalytic strategy facilitating transition state formation through hydrogen bond formation and electrostatic bond formation between the substrate and enzyme active site.

Answer 19

A catalytic strategy facilitating transition state formation through interaction involving metal ions and substrate in the enzyme active site.

Answer 20

A catalytic strategy facilitating transition state formation through direct transfer of a proton to or from the substrate in the enzyme active site.

Answer 21

Half of Vmax

Answer 22

Two thirds of Vmax

Answer 23

Double Vmax

Answer 24

Three times Vmax

Answer 25

May explain why enzymes have particular substrate specificity.

Answer 26

May explain why enzymes are able to catalyse chemical reactions that cannot be facilitated in any other way

Answer 27

May explain why enzymes increase the rate of a reaction by reduction of the activation energy change for the reaction

Answer 28

May explain why enzymes can effectively reduce the loss of energy from a chemical reaction as heat

Answer 29

are chemically altered at the end of their reaction

Answer 30

are involved in changing the equilibrium constant of the reaction that they catalyse

Answer 31

bind their substrates at their active site(s)

Answer 32

increase the activation energy of the reaction they catalyse

Answer 33

Is a measure of the rate acceleration caused by the enzyme

Answer 34

For a given enzyme is independent of the substrate used

Answer 35

Has units of concentration

Answer 36

Gives an idea of the enzyme’s catalytic efficiency

Answer 37

Is altered when a competitive inhibitor is present

Answer 38

Can be determined from the intercept on the x-axis of a Lineweaver-Burk plot

Answer 39

Is the maximum rate at which the enzyme can convert substrate into product

Answer 40

Has units of concentration

Answer 41

Is controlled by serine protease enzymes.

Answer 42

Is a key part of the control mechanism in the eukaryote cell cycle

Answer 43

Is a key part of the control mechanism in the prokaryote cell cycle

Answer 44

Is controlled by ubiquinone activating enzymes.

Answer 45

Is completely located in the mitochondrial matrix.

Answer 46

Facilitates transport of ammonia produced in the liver to the muscles where it can be used in anabolic processes - preventing the exposure of free ammonium to other components of eukaryote tissues.

Answer 47

Facilitates transport of ammonia produced in the muscles to the liver where it can be effectively removed from the body - preventing the exposure of free ammonium to other components of eukaryote tissues.

Answer 48

Is located in the cell membrane of muscle cells.

Answer 49

Describes the way the substrate interacts with the enzyme.

Answer 50

Descibes the protein tertiary structure when the enzyme substrate is converted to a product.

Answer 51

Describes the form the substrate takes that facilitates the formation of a low energy intermediate during the catalytic cycle.

Answer 52

Describes an intermediate in the catalytic cycle that is produced in order to minimise the activation energy for the reaction.

Answer 53

Will always be negative if an enzyme catalysed reaction proceeds spontaneously.

Answer 54

Will always be positive if an enzyme catalysed reaction proceeds spontaneously.

Answer 55

Will always be equal to the ΔG value for a reaction where both the reactants and products have an equal concentration.

Answer 56

Will only apply to a reaction occurring if the pH = 7.0 in aqueous solution.

Answer 57

An enzyme that is protein-engineered to work like an antibody.

Answer 58

An antibody that is protein-engineered to work like an enzyme.

Answer 59

An enzyme that has high affinity for a transition state analogue.

Answer 60

An antibody that has high affinity for a transition state analogue.

Answer 61

A region of the enzyme active site that facilitates binding of positively charged substrates through their association with oxygen-containing amino-acid side chains in the enzyme.

Answer 62

A region of the enzyme active site that facilitates binding of negatively charged substrates through their association with oxygen-containing amino- acid side chains in the enzyme.

Answer 63

A region of the active site that facilitates binding of positively charged oxygen- containing groups present in a substrate.

Answer 64

A region of the active site that facilitates binding of negatively charged oxygen-containing groups present in a substrate.

Answer 65

Approximation.

Answer 66

Acid-base catalysis.

Answer 67

Metal-ion catalysis.

Answer 68

Covalent catalysis.

Answer 69

Is completely located in the mitochondrial matrix – preventing the exposure of free ammonium to other components of the eukaryote cell.

Answer 70

Allows free ammonia obtained directly from deamination of glutamate to be converted to urea – preventing the exposure of free ammonium to other components of the eukaryote cell.

Answer 71

Allows free ammonia obtained directly from deamination of tryptophan to be converted to urea – preventing the exposure of free ammonium to other components of the eukaryote cell.

Answer 72

Is completely located in the cytoplasm of the cell – preventing the exposure of free ammonium to other components of the eukaryote cell.

Answer 73

Active site

Answer 74

Activation site

Answer 75

Allosteric site

Answer 76

Transitional site

Answer 77

Are proteases that hydrolyse polypeptides with serine in the F1 position

Answer 78

Are proteases that are found in the cytoplasm of all cells

Answer 79

Utilise a serine residue at the active site to facilitate substrate binding

Answer 80

Utilise a serine residue at the active site to facilitate cleavage of peptide bonds

Answer 81

An acidic- or basic- amino acid in the active site of an enzyme facilitates transition state formation by hydrogen abstraction from an appropriate substrate.

Answer 82

An acid- or basic- substrate in the active site of an enzyme facilitates transition state formation by hydrogen abstraction from a catalytic amino acid in the active site.

Answer 83

Both are correct.

Answer 84

Neither are correct.

Answer 85

Can be covalently linked to proteins via the N-terminus glycine residue.

Answer 86

Is a polypeptide.

Answer 87

Is an essential component of eukaryote respiratory chains.

Answer 88

Can be covalently linked to proteins via isopeptide bond formation.

Answer 89

The reaction will proceed fast with the formation of the explosive products.

Answer 90

The reaction will not occur spontaneously.

Answer 91

The reaction will never reach equilibrium.

Answer 92

The reaction will proceed spontaneously from left to right.

Answer 93

Is a key concept that helps to explain how enzymes reduce activation energy for chemical reactions.

Answer 94

Is a key concept that helps to explain how enzymes can reduce the Gibb’s free energy for a chemical reaction.

Answer 95

Is a key concept that helps to explain how enzymes can exhibit diverse substrate specificity.

Answer 96

Is a key concept that helps to explain how enzymes may exhibit Michaelis-Menton kinetics.

Answer 97

Is a term used to describe the amount of randomness or disorder that results as the reaction proceeds

Answer 98

Is a term used to describe the amount of ‘free energy’ change that results as the reaction proceeds

Answer 99

Is a term used to describe the amount of heat that is produced or consumed as the reaction proceeds

Answer 100

Is always determined at room temperature (25oC)

Answer 101

Facilitate substrate binding

Answer 102

Facilitate transition state formation

Answer 103

Facilitate stabilisation of the tertiary structure

Answer 104

Facilitate conformational changes in the protein during the catalytic cycle

Answer 105

Reduce the entropy associated with chemical reactions

Answer 106

Reduce the enthalpy associated with chemical reactions

Answer 107

Reduce the Gibb’s free energy associated with chemical reactions

Answer 108

Reduce the activation energy associated with chemical reactions

Answer 109

Reaction 1

Answer 110

Reaction 2

Answer 111

They both occur at much the same rate

Answer 112

It is not possible to know this from the data provided

Answer 113

Can be described by the ratio: kCAT/KM

Answer 114

Can be described by the ratio: KM/kCAT

Answer 115

Can be described by the ratio: Vmax/kCAT

Answer 116

Can be described by the ratio: kCAT/Vmax

Answer 117

Hydrogen bonding with at least one amino acid side chain at the active site to facilitate formation of the transition state.

Answer 118

Hydrogen bonding between the carbonyl and amide groups of peptide bonds to facilitate formation of the transition state.

Answer 119

Hydrogen bonding between a water molecule and the substrate to facilitate formation of the transition state.

Answer 120

Hydrogen bonding with an oxidised metal ion prosthetic group in the active site to facilitate formation of the transition state.

Answer 121

The reaction will stop

Answer 122

The reaction will proceed spontaneously from B to A

Answer 123

The reaction will proceed spontaneously from A to B

Answer 124

The reaction will not occur spontaneously

Answer 125

This reaction can only occur in a cell in which NADH is converted to NAD+ by the respiratory chain

Answer 126

This reaction can only occur in a cell if it is coupled to another reaction for which ΔG°' is large and negative

Answer 127

This reaction may occur in cells at some concentrations of substrate and product

Answer 128

This reaction is energy-releasing

Answer 129

Is always the rate limiting step in an enzyme catalysed reaction

Answer 130

Is never the rate limiting step in an enzyme catalysed reaction

Answer 131

Is always a necessary pre-requisite to formation of the transition state and therefore product turnover

Answer 132

Is never a necessary pre-requisite to formation of the transition state and therefore product turnover

Answer 133

alter the Vmax of the reaction

Answer 134

show irreversible binding to their target enzyme

Answer 135

resemble the structure of the natural substrate/product molecule

Answer 136

bind at a site distant from the active site

Answer 137

Inhibits proteosome-mediated protein degradation

Answer 138

Is essential for proteosome-mediated protein degradation

Answer 139

Enhances proteosome-mediated protein degradation

Answer 140

Has nothing to do with proteosome-mediated protein degradation

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Enzymes/N-metabolism Years 2013-2009

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