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Enzymes

Enzymes
99問 • 1年前
  • Miguel Inigo Garcia
    • 通報

    問題一覧

  • 1

    All eznymes are proteins

    False

  • 2

    Redox reactions

    Oxidoreductases

  • 3

    Transfer of moieties (glycosyl, methyl, phosphoryl groups)

    Transferases

  • 4

    Hydrolytic cleavage of C-C, C-O, C-N, and other COVALENT BONDS

    Hydrolases

  • 5

    Catalyzes geometric or structural changes within a molecule

    Isomerases

  • 6

    Joining together of 2 molecules in reactions coupled to the HYDROLYSIS OF ATP

    Ligases

  • 7

    Catalyze oxidation-reduction reactions (Lactate -> Pyruvate)

    Oxidoreductases

  • 8

    Catalyze transfer of C-, N-, or P- containing groups (Serine -> Glycine)

    Transferases

  • 9

    Catalyzes cleavage of bonds by addition of water (Urea + H2O -> CO2 + 2 NH3)

    Hydrolases

  • 10

    Catalyzes cleavage of C-C, C-S, and certain C-N bonds (Pyruvate -> Acetaldehyde)

    Lyases

  • 11

    Cleavage of COVALENT BONDS by ATOM ELIMINATION, generating DOUBLE BONDS

    Lyases

  • 12

    Catalyze rearrangement of optical or geometric isomers (Methylmalonyl CoA -> Succinyl CoA)

    Isomerases

  • 13

    Catalyzes formation of bonds between Carbon and O, S, and N coupled to HYDROLYSIS OF HIGH-ENERGY PHOSPHATES (Pyruvate -> Oxaloacetate)

    Ligases

  • 14

    TIGHT AND STABLY INCORPORATED into a protein’s structure by COVALENT BONDS or NONCOVALENT FACTORS

    Prosthetic groups

  • 15

    Bind weakly and transiently to their cognate enzymes or substrates (dissociable complexes)

    Cofactors

  • 16

    Small organic molecules

    Coeznymes

  • 17

    Pyridoxal phosphate, Flavin mononucleotide (FMN), and Flavin adenine dinucleotide (FAD)

    Prosthetic groups

  • 18

    Thiamine pyrophosphate, Lipoic acid, and Biotin

    Prosthetic groups

  • 19

    Transition metals (Fe, Co, Cu, Mg, Mn, and Zn)

    Prosthetic groups

  • 20

    Metalloenzymes

    Prosthetic groups

  • 21

    Metal ions and metal activated enzymes

    Cofactors

  • 22

    Derived from water-soluble B vitamins

    Coenzymes

  • 23

    NAD and NADP - nicotinamide

    Coenzymes

  • 24

    FMN and FAD - riboflavin

    Coenzymes

  • 25

    Coenzyme A - pantothenic acid

    Coenzymes

  • 26

    An active enzyme with its nonprotein moiety

    Holoenzyme

  • 27

    An enzyme without its nonprotein moiety

    Apoenzyme

  • 28

    Association between enzyme and substrate is

    Temporary

  • 29

    The higher the concentration, the more frequently substrates wiill encounter one another; hence, the rate at which reaction products appear will be greater.

    Catalysis by proximity

  • 30

    Ionizable functional groups of aminoacyl side chains contribute to catalysis by acting as acids or bases

    Acid-base catalysis

  • 31

    Participating acids or bases are protons or hydroxide ions

    Specific acid or base catalysis

  • 32

    Independent of the concentration of other acids or bases in the active site

    Specific acid or base catalysis

  • 33

    Reactions whose rates are responsive to all acids or bases present

    Specific acid or base catalysis

  • 34

    Creates conformational change in an enzyme that weakens the bond through physical distortion and electronic polarization

    Catalysis by strain

  • 35

    Transition state intermediate - strained conformation

    Catalysis by strain

  • 36

    Formation of covalent bonds between enzymes and one or more substrates

    Covalent catalysis

  • 37

    MOdified enzyme becomes a reactant

    Covalent catalysis

  • 38

    Follows ping pong mechanism

    Covalent catalysis

  • 39

    First substrate is bound and its product is released prior to the bonding of the second substrate

    Ping pong mechanism

  • 40

    Exquisite specificity of enzyme-substrate interactions

    Fischer’s lock and key model

  • 41

    Substrates bind to an enzyme inducing conformational changes that is naalogous to placing a hand (substrate) into a glove (enzyme)

    Daniel Koshland’s induced fit model

  • 42

    Change/ time

    Rate

  • 43

    Formation of product/ period of time

    Reaction rate

  • 44

    According to the Kinetic Theory/ Collision theory: Molecules must approach within _____ distance of one another to collide

    bond-forming

  • 45

    According to the Kinetic Theory/ Collision theory: Molecules must possess sufficient _____ to overcome the energy barrier for reaching the _____.

    kinetic energy; transition state

  • 46

    Describes: 1. The direction in which a chemical reaction will tend to proceed 2. The concentrations of reactants and products that will be present at equilibrium

    Gibbs free-energy change

  • 47

    In Gibbs free-energy change, enzymes affect the equilibrium constant and free energy for the overall reaction

    False

  • 48

    K eq = [P] [Q] / [A] [B]

    Gibbs free-energy change

  • 49

    If change in G is a NEGATIVE number, K eq will be _____ than unity; and the concentration of products will _____ that of the substrates

    Greater; exceed

  • 50

    If G is a positive number, K eq will be _____ than unity, and the formation of _____ will be favoured

    Less; substrates

  • 51

    Difference in free energy between the reactant and transition state

    Activation energy

  • 52

    Free energy dictates the _____ of chemical reactions

    Direction

  • 53

    Activation energy dictates the _____ of reactions

    Rate

  • 54

    High activation energy in uncatalyzed reaction results in

    Slow reaction rate

  • 55

    Lower activation energy results in

    Faster rate of reaction

  • 56

    More molecules have sufficient energy to pass through the transition state

    Lower activation energy

  • 57

    Enzymes provide alternation reaction pathways that _____ activation energy; _____ free energy of substrates and products

    Lowers; does not affect

  • 58

    Rate of an enzyme catalyzed reaction _____ with substrate concentration until a maximal _____ is reached

    Increases; velocity

  • 59

    Increasing temperature ______ the rate of both uncatalyzed and enzyme-catalyzed reactions by _____ kinetic energy and the collision frequency of reaction molecules

    Increases; increasing

  • 60

    _____ temperatures will result to denaturation, resulting in _____ of the catalytic activity

    Higher; loss

  • 61

    In the Michaelis-Menten equation, substrate concentration is _____ enzyme concentration

    Greater than

  • 62

    In the Michaelis-Menten equation, concentration of the ES complex _____ with time

    Does not change

  • 63

    Used to determine mechanism of action of enzyme inhibitors

    Lineweaver Burk Plot

  • 64

    Reversible enzyme inhibitors

    Noncovalent bonds

  • 65

    Irreversible enzyme inhibitors

    Covalent bonds

  • 66

    Inhibitor binds reversibly to the same site that the substrate would normally occupy

    Competitive inhibition

  • 67

    Vmax = unchanged (increasing S will reach the Vmax observed in the absence of the inhibitor)

    Competitive inhibition

  • 68

    K = increases

    Competitive inhibtion

  • 69

    Inhibited and uninhibited reactions intersect on y axis (at 1/Vmax) and different x intercepts at -1/Km

    Competitive inhibition

  • 70

    Example = HMG CoA reductase inhibitors

    Competitive inhibitor

  • 71

    Inhibitor and substrate bind at different sites on the enzyme

    Noncompetitive inhibition

  • 72

    Vmax = decreases apparent Vmax of reaction

    Noncompetitive inhibition

  • 73

    Km = unchanged

    Noncompetitive inhibition

  • 74

    Oxypurinol is a _____ of xanthine oxidase

    Noncompetitive inhibitor

  • 75

    In allosteric enzymes, the effectors bind _____ noncovalently at _____

    Noncovalently; a site other than the active site

  • 76

    Substrates as effector

    Homotropic effectors

  • 77

    Functions as positive effector

    Homotropic effector

  • 78

    Sigmoidal curve

    Homotropic effector

  • 79

    Positive cooperativity

    Homotropic effector

  • 80

    Example: hemoglobin

    Homotropic effector

  • 81

    Effectors different from substrate

    Heterotropic effector

  • 82

    Feedback inhibition

    Heterotropic effector

  • 83

    Phosphofructokinase-1 is allosterically inhibited by citrate

    Heterotropic effector

  • 84

    Protein kinases; use ATP as phosphate donor

    Phosphorylation

  • 85

    Activates the enzyme

    Phosphorylation

  • 86

    Phosphoprotein kinase

    Dephosphorylation

  • 87

    Deactivates the enzyme

    Dephosphorylation

  • 88

    Typical effector of substrate availability

    Substrate

  • 89

    Typical effector of product inhibition

    Reaction Product

  • 90

    Typical effector of allosteric control

    Pathway end product

  • 91

    Typical effector of covalent modification

    Another enzyme

  • 92

    Typical effector of synthesis or degradation of enzyme

    Hormone or metabolite

  • 93

    Results of substrate availability

    Change in velocity

  • 94

    Results in a change in Vmax and/ or Km

    Product inhibition and Covalent modification

  • 95

    Results in a change in Vmax and/ or K 0.5

    Allosteric control

  • 96

    Results in a change in the amount of enzyme

    Synthesis or degradation of enzyme

  • 97

    Time required for substrate availability, product inhibition, and allosteric control

    Immediate

  • 98

    Time required for change for Covalent modification

    Immediate to minutes

  • 99

    Time required for synthesis or degradation of enzymes

    Hours to days

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    問題一覧

  • 1

    All eznymes are proteins

    False

  • 2

    Redox reactions

    Oxidoreductases

  • 3

    Transfer of moieties (glycosyl, methyl, phosphoryl groups)

    Transferases

  • 4

    Hydrolytic cleavage of C-C, C-O, C-N, and other COVALENT BONDS

    Hydrolases

  • 5

    Catalyzes geometric or structural changes within a molecule

    Isomerases

  • 6

    Joining together of 2 molecules in reactions coupled to the HYDROLYSIS OF ATP

    Ligases

  • 7

    Catalyze oxidation-reduction reactions (Lactate -> Pyruvate)

    Oxidoreductases

  • 8

    Catalyze transfer of C-, N-, or P- containing groups (Serine -> Glycine)

    Transferases

  • 9

    Catalyzes cleavage of bonds by addition of water (Urea + H2O -> CO2 + 2 NH3)

    Hydrolases

  • 10

    Catalyzes cleavage of C-C, C-S, and certain C-N bonds (Pyruvate -> Acetaldehyde)

    Lyases

  • 11

    Cleavage of COVALENT BONDS by ATOM ELIMINATION, generating DOUBLE BONDS

    Lyases

  • 12

    Catalyze rearrangement of optical or geometric isomers (Methylmalonyl CoA -> Succinyl CoA)

    Isomerases

  • 13

    Catalyzes formation of bonds between Carbon and O, S, and N coupled to HYDROLYSIS OF HIGH-ENERGY PHOSPHATES (Pyruvate -> Oxaloacetate)

    Ligases

  • 14

    TIGHT AND STABLY INCORPORATED into a protein’s structure by COVALENT BONDS or NONCOVALENT FACTORS

    Prosthetic groups

  • 15

    Bind weakly and transiently to their cognate enzymes or substrates (dissociable complexes)

    Cofactors

  • 16

    Small organic molecules

    Coeznymes

  • 17

    Pyridoxal phosphate, Flavin mononucleotide (FMN), and Flavin adenine dinucleotide (FAD)

    Prosthetic groups

  • 18

    Thiamine pyrophosphate, Lipoic acid, and Biotin

    Prosthetic groups

  • 19

    Transition metals (Fe, Co, Cu, Mg, Mn, and Zn)

    Prosthetic groups

  • 20

    Metalloenzymes

    Prosthetic groups

  • 21

    Metal ions and metal activated enzymes

    Cofactors

  • 22

    Derived from water-soluble B vitamins

    Coenzymes

  • 23

    NAD and NADP - nicotinamide

    Coenzymes

  • 24

    FMN and FAD - riboflavin

    Coenzymes

  • 25

    Coenzyme A - pantothenic acid

    Coenzymes

  • 26

    An active enzyme with its nonprotein moiety

    Holoenzyme

  • 27

    An enzyme without its nonprotein moiety

    Apoenzyme

  • 28

    Association between enzyme and substrate is

    Temporary

  • 29

    The higher the concentration, the more frequently substrates wiill encounter one another; hence, the rate at which reaction products appear will be greater.

    Catalysis by proximity

  • 30

    Ionizable functional groups of aminoacyl side chains contribute to catalysis by acting as acids or bases

    Acid-base catalysis

  • 31

    Participating acids or bases are protons or hydroxide ions

    Specific acid or base catalysis

  • 32

    Independent of the concentration of other acids or bases in the active site

    Specific acid or base catalysis

  • 33

    Reactions whose rates are responsive to all acids or bases present

    Specific acid or base catalysis

  • 34

    Creates conformational change in an enzyme that weakens the bond through physical distortion and electronic polarization

    Catalysis by strain

  • 35

    Transition state intermediate - strained conformation

    Catalysis by strain

  • 36

    Formation of covalent bonds between enzymes and one or more substrates

    Covalent catalysis

  • 37

    MOdified enzyme becomes a reactant

    Covalent catalysis

  • 38

    Follows ping pong mechanism

    Covalent catalysis

  • 39

    First substrate is bound and its product is released prior to the bonding of the second substrate

    Ping pong mechanism

  • 40

    Exquisite specificity of enzyme-substrate interactions

    Fischer’s lock and key model

  • 41

    Substrates bind to an enzyme inducing conformational changes that is naalogous to placing a hand (substrate) into a glove (enzyme)

    Daniel Koshland’s induced fit model

  • 42

    Change/ time

    Rate

  • 43

    Formation of product/ period of time

    Reaction rate

  • 44

    According to the Kinetic Theory/ Collision theory: Molecules must approach within _____ distance of one another to collide

    bond-forming

  • 45

    According to the Kinetic Theory/ Collision theory: Molecules must possess sufficient _____ to overcome the energy barrier for reaching the _____.

    kinetic energy; transition state

  • 46

    Describes: 1. The direction in which a chemical reaction will tend to proceed 2. The concentrations of reactants and products that will be present at equilibrium

    Gibbs free-energy change

  • 47

    In Gibbs free-energy change, enzymes affect the equilibrium constant and free energy for the overall reaction

    False

  • 48

    K eq = [P] [Q] / [A] [B]

    Gibbs free-energy change

  • 49

    If change in G is a NEGATIVE number, K eq will be _____ than unity; and the concentration of products will _____ that of the substrates

    Greater; exceed

  • 50

    If G is a positive number, K eq will be _____ than unity, and the formation of _____ will be favoured

    Less; substrates

  • 51

    Difference in free energy between the reactant and transition state

    Activation energy

  • 52

    Free energy dictates the _____ of chemical reactions

    Direction

  • 53

    Activation energy dictates the _____ of reactions

    Rate

  • 54

    High activation energy in uncatalyzed reaction results in

    Slow reaction rate

  • 55

    Lower activation energy results in

    Faster rate of reaction

  • 56

    More molecules have sufficient energy to pass through the transition state

    Lower activation energy

  • 57

    Enzymes provide alternation reaction pathways that _____ activation energy; _____ free energy of substrates and products

    Lowers; does not affect

  • 58

    Rate of an enzyme catalyzed reaction _____ with substrate concentration until a maximal _____ is reached

    Increases; velocity

  • 59

    Increasing temperature ______ the rate of both uncatalyzed and enzyme-catalyzed reactions by _____ kinetic energy and the collision frequency of reaction molecules

    Increases; increasing

  • 60

    _____ temperatures will result to denaturation, resulting in _____ of the catalytic activity

    Higher; loss

  • 61

    In the Michaelis-Menten equation, substrate concentration is _____ enzyme concentration

    Greater than

  • 62

    In the Michaelis-Menten equation, concentration of the ES complex _____ with time

    Does not change

  • 63

    Used to determine mechanism of action of enzyme inhibitors

    Lineweaver Burk Plot

  • 64

    Reversible enzyme inhibitors

    Noncovalent bonds

  • 65

    Irreversible enzyme inhibitors

    Covalent bonds

  • 66

    Inhibitor binds reversibly to the same site that the substrate would normally occupy

    Competitive inhibition

  • 67

    Vmax = unchanged (increasing S will reach the Vmax observed in the absence of the inhibitor)

    Competitive inhibition

  • 68

    K = increases

    Competitive inhibtion

  • 69

    Inhibited and uninhibited reactions intersect on y axis (at 1/Vmax) and different x intercepts at -1/Km

    Competitive inhibition

  • 70

    Example = HMG CoA reductase inhibitors

    Competitive inhibitor

  • 71

    Inhibitor and substrate bind at different sites on the enzyme

    Noncompetitive inhibition

  • 72

    Vmax = decreases apparent Vmax of reaction

    Noncompetitive inhibition

  • 73

    Km = unchanged

    Noncompetitive inhibition

  • 74

    Oxypurinol is a _____ of xanthine oxidase

    Noncompetitive inhibitor

  • 75

    In allosteric enzymes, the effectors bind _____ noncovalently at _____

    Noncovalently; a site other than the active site

  • 76

    Substrates as effector

    Homotropic effectors

  • 77

    Functions as positive effector

    Homotropic effector

  • 78

    Sigmoidal curve

    Homotropic effector

  • 79

    Positive cooperativity

    Homotropic effector

  • 80

    Example: hemoglobin

    Homotropic effector

  • 81

    Effectors different from substrate

    Heterotropic effector

  • 82

    Feedback inhibition

    Heterotropic effector

  • 83

    Phosphofructokinase-1 is allosterically inhibited by citrate

    Heterotropic effector

  • 84

    Protein kinases; use ATP as phosphate donor

    Phosphorylation

  • 85

    Activates the enzyme

    Phosphorylation

  • 86

    Phosphoprotein kinase

    Dephosphorylation

  • 87

    Deactivates the enzyme

    Dephosphorylation

  • 88

    Typical effector of substrate availability

    Substrate

  • 89

    Typical effector of product inhibition

    Reaction Product

  • 90

    Typical effector of allosteric control

    Pathway end product

  • 91

    Typical effector of covalent modification

    Another enzyme

  • 92

    Typical effector of synthesis or degradation of enzyme

    Hormone or metabolite

  • 93

    Results of substrate availability

    Change in velocity

  • 94

    Results in a change in Vmax and/ or Km

    Product inhibition and Covalent modification

  • 95

    Results in a change in Vmax and/ or K 0.5

    Allosteric control

  • 96

    Results in a change in the amount of enzyme

    Synthesis or degradation of enzyme

  • 97

    Time required for substrate availability, product inhibition, and allosteric control

    Immediate

  • 98

    Time required for change for Covalent modification

    Immediate to minutes

  • 99

    Time required for synthesis or degradation of enzymes

    Hours to days