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BIOC3021 > Enzyme Regulation > Flashcards

Enzyme Regulation Flashcards

1
Q

_____ ______ bind to the same site of the enzyme, the active site

A

competitive inhibitors

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2
Q

____ _____ bind from a different site than the active site and bring about conformational change

A

noncompetitive inhibitors

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3
Q

____ inhibitors decrease Kcat and change substrate binding (Km)

A

mixed

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4
Q

_____ inhibitors decrease Kcat but do not affect substrate binding

A

pure

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5
Q

what are the two types of noncompetitive inhibitors?

A

mixed and pure

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6
Q

A competitive inhibitor is similar in ___ and ____ to the normal subsrate

A

size, shape

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7
Q

A competitive inhibitor cannot undergo a ___ _____

A

chemical reaction

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8
Q

Inhibitors might make it so the substrate is ____ bound to the enzyme

A

loosely

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9
Q

Inhibitors decrease the ____ of the substrate/reaction

A

Vmax

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10
Q

The inhibitors binds irreversibly to the enzyme by ____ bonds

A

covalent

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11
Q

____ substrates generate a reactive group that forms a covalent bond during binding to the active site

A

suicide

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12
Q

Penicillin is an example of a ____ substrate

A

suicide

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13
Q

Penicillin forms a covalent bond with an enzyme involved in the synthesis of what?

A

bacterial cell walls

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14
Q

Enzyme ____ is the ability of an enzyme to catalyze one particular reaction

A

specificity

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15
Q

What hypothesis considers the enzyme as the lock and the substrate fits in as the key?

A

lock and key

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16
Q

What hypothesis considers that the enzyme’s active site is modified upon binding to the substrate?

A

induced fit

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17
Q

The substrate glucose is bound to the active site of what enzyme?

A

hexokinase

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18
Q

What are the four mechanisms of enzyme regulation?

A

genetic control, covalent modification, specialized controls, allosteric regulation

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19
Q

___ _____ is the amount of enzyme that is produced by a gene (whether the gene for the enzyme is present, permanently suppressed, etc.)

A

genetic control

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20
Q

___ ______ is the attachment of chemical groups such as phosphate groups

A

covalent modification

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21
Q

Zymogens, isozymes, and modular proteins are examples of what?

A

specialized controls

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22
Q

___ _____ is an inhibitor of activator binding to the enzyme at a site different than the active site

A

allosteric regualation

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23
Q

What donates the phosphate molecule in the attachment of a phosphate group via covalent modification?

A

ATP

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24
Q

Protein ____ is an enzyme that adds a phosphate group to an enzyme

A

kinase

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25
Q

protein ____ is an enzyme that removes a phosphate group from an enzyme

A

phosphatase

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26
Q

The enzyme is catalytically active when the phosphate is ____

A

removed

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27
Q

The enzyme is catalytically inactive when the phosphate is _____

A

attached

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28
Q

The phosphate group addition affects protein _____

A

folding

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29
Q

The ___ ____ ____-_____ is removed from the enzyme when adding a phosphate group

A

amino acid side-chain

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30
Q

Phosphate ____ the active site of an enzyme, making it inactive

A

closes

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31
Q

_____ are inactive precursors of enzymes or other proteins that acquire full activity by specific cleavage of one or more peptide bonds of the proteins

A

zymogens

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32
Q

insulin, proteolytic enzymes, and blood clotting factors are examples of what?

A

zymogens

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33
Q

_____ is generated by excision of a specific peptide from proinsulin

A

insulin

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34
Q

_____ is the active form of proinsulin

A

insulin

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35
Q

Insulin is the active form of _____

A

proinsulin

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36
Q

_____ _____ are synthesized as zymogens in the pancreas and stomach

A

prteolytic

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37
Q

__ ___ ____ are produced by activation of zymogens of clotting factors

A

blood clotting factors

38
Q

Proteolytic enzymes break down what?

A

dietary protein

39
Q

Insulin is activated by the ____ of specific peptides

A

removal

40
Q

Trypsin originates in the ___

A

pancreas

41
Q

Chymotrypsin originates in the _____

A

panceras

42
Q

Chymotrypsin originates in the _____

A

pancreas

43
Q

Carboxypeptidase originates in the _____

A

pancreas

44
Q

Elastase originates in the ____

A

pancreas

45
Q

Pepsin originates in the _____

A

stomach

46
Q

what is the active protein of trypsinogen?

A

trypsin

47
Q

what is the active protein of chymotrypsinogen?

A

chymotrypsin

48
Q

what is the active protein of procarboxypeptidase?

A

carboxypetidase

49
Q

what is the active protein of proelastase?

A

elastase

50
Q

what is the active protein of pepsinogen?

A

pepsin

51
Q

What is the zymogen of trypsin?

A

trypsinogen

52
Q

What is the zymogen of chymotrypsin?

A

chymotrypsinogen

53
Q

What is the zymogen of carboxypeptidase?

A

procarboxypeptidase

54
Q

What is the zymogen of elastase?

A

proelastase

55
Q

What is the zymogen of pepsin?

A

pepsinogen

56
Q

In the proteolytic activation of chymotrypsinogen, peptide bonds are _____ at the ends

A

cut

57
Q

Chymotrypsin attacks _____ in the proteolytic activation process

A

itself

58
Q

___ chymotrypsin is the fully active form

A

alpha

59
Q

Chymotrypsin’s proteins are connected by what type of bonds?

A

disulfide bonds

60
Q

What are the two blood clot formation pathways?

A

extrinsic/tissue factor, intrinsic/contact activation

61
Q

Fibrinogen is ___ in blood

A

soluble

62
Q

Fibrin is ______ in blood

A

insoluble

63
Q

Fibrin forms ___ ____

A

blood clots

64
Q

_______ activates blood clotting factors in the intrinsic pathway

A

proteases

65
Q

_____ are forms of an enzyme that differ in their quaternary structure with different numbers of distinct polypeptide units

A

isozymes

66
Q

Lactate dehydrogenase is an example of what ?

A

isozyme

67
Q

There are ____ different subunits of LDH

A

5

68
Q

____ _____ LDH is mainly A4 isozyme

A

skeletal muslce

69
Q

Skeletal muscle LDH produces ____ ______ in ____ conditions

A

lactic acid, anaerobic

70
Q

___ ____ LDH is mainly B4 isozyme

A

heart muscle

71
Q

Heart muscle LDH uses ___ ____ in _____ conditions

A

lactic acid, aerobic

72
Q

The two isozymes of LDH work in ____ directions

A

opposite

73
Q

___ ____ are proteins that bind to enzymes and influence their activity

A

modulator proteins

74
Q

modulator proteins ___ ___ the active site of enzymes

A

cover up

75
Q

cAMP dependent protein kinases are examples of what?

A

modulator proteins

76
Q

in cAMP dependent protein kinases, catalytic subunits are what part?

A

the enzyme

77
Q

in cAMP dependent protein kinases, regulatory subunits are what part?

A

modulator proteins (that bind to the C subunits)

78
Q

in cAMP dependent protein kinases, the R subunits ______ C subunit activity

A

inhibit

79
Q

The modulator protein prevents ____ from binding to the active site and therefore stops product molecules from being made

A

substrates

80
Q

cAMP dependent protein kinase is active when R subunits are _____

A

disconnected

81
Q

___ ____ is the inhibition or activation of enzyme activity through noncovalent binding of small molecules to a site different than the active site

A

allosteric regulation

82
Q

____ _____ is when the final product binds to the first enzyme to prevent further synthesis of the product

A

feedback inhibition

83
Q

Feedback inhibition is what type of reguation?

A

non-competitive

84
Q

What is the graph shape of allosteric enzymes?

A

sigmoid/S shaped curves

85
Q

What is the s shaped curve of allosteric enzymes caused by?

A

cooperative binding

86
Q

For an allosteric enzyme, the binding of the first substrate molecule makes it ______ for other substrate molecules to bind to different subunits

A

easier

87
Q

Allosteric effectors change the ______ structure of the subunit polypeptides and/or change the subunit interactions

A

3D

88
Q

For an allosteric enzyme, the more substrate there is the more ____ states are converted into the ___ state

A

T (taut), R (relaxed)

89
Q

For allosteric enzymes, the ___ state is inactive

A

T (taut)

90
Q

For allosteric enzymes, the ___ state is active

A

R (relaxed)

91
Q

A dimeric protein is how many subunits?

A

2

BIOC3021 (25 decks)

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