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Biochem Lec MID-TERMS > Enzymes > Flashcards

Enzymes Flashcards

1
Q

_________ is also called as Biological catalysts

A

Enzymes

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2
Q

Enzymes increases the rate of reactions by a factor between ____ to ______ times

A

10^6, 10^12

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3
Q

most enzymes are ________

A

Proteins

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4
Q

It is nomenclature

A

Enzymes

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5
Q

______ is not used up in reactions

A

Enzymes

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6
Q

Enzymes is highly ______

A

Specific

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7
Q

Enzymes is chemically recognize, it _____and ______

A

Bind, modify substrates

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8
Q

Enzymes is high ______ weight compounds made up principally of chains of ______ linked together by _____ bonds

A

Molecular, amino acids, peptide

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9
Q

Enzymes can be ______ and _____ with salts, solvents and other Reagents

A

Denatured, Precipitated

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10
Q

Enzymes can be denatured and precipitated with _____, _____ and ____

A

Salt, solvents, other Reagents

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11
Q

Enzymes require the presence of other compound- ______ before their _______ activity can be exerted

A

Cofactor, catalytic

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12
Q

What are the different types of enzymes classes

A

Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases

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13
Q

Is a class of enzyme that transfer electrons (hydride ions or H atoms)

A

Oxidoreductases

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14
Q

Is a class of enzyme that is involved in group transfer reactions

A

Transferases

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15
Q

Is a class of enzyme that involved in hydrolysis of reactions (transfer of functional group to water)

A

Hydrolases

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16
Q

In Hydrolases it involves the transfer of _____ groups to _____

A

Functional, water

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17
Q

Is a class of enzyme which form double bonds by removal of groups

A

Lyases

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18
Q

Is a class of enzyme that transfer of groups within the molecules to yield isomeric forms

A

Isomerases

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19
Q

Is a class of enzyme that form C-C, C-S, C-O and C-N bonds by condensation reactions coupled to ATP cleavage.

A

Ligases

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20
Q

In Ligases, enzyme that form C-C, C-S, C-O and C-N bonds by _____ reactions coupled to ____ cleavage.

A

Condensation, ATP

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21
Q

In Ligases what bonds is formed due to condensation reaction

A

C-C
C-S
C-O
C-N

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22
Q

Enzymes are highly ______ : they catalyze only ____ reaction, having a specific substrate. This specificity results from an enzymes specific three dimensional shape.

A

Specific, one

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23
Q

The specificity of enzymes results to form what shape

A

Specific 3 dimensional shape

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24
Q

What do you call to a part of enzyme that binds to the substrate

A

Active site

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25
Q

The three dimensional shape of the molecule to be reacted is called

A

Substrate

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26
Q

What is formed when the substrate and enzyme bind temporarily

A

Enzyme-substrate complex

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27
Q

The activation energy needed for the reaction to occur is ____

A

Reduced

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28
Q

After the reaction is _____ the substrate has formed a new ______ and enzyme is _____ to be _____

A

Complete, product, released, reused

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29
Q

What are the two main reasons why an enzyme is regulated

A

•it is a waste of energy if the cell continues sleep produce a large amount of enzyme even when the amount of substrate is very low
•if the amount of product from the enzyme catalyzed reaction is already more than what the cell needs

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30
Q

The enzyme must be turned ___ to be regulated

A

Off

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31
Q

What are the two enzyme action

A

Lock and key model
Induced fit model

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32
Q

It is a type of enzyme action that the substrate molecule has a specific 3 dimensional shape that allows it to fit of an enzymes active site.

A

Lock and key model

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33
Q

A type of enzyme action that interaction between the enzyme and substrate induces or changes the shape of the molecule to produce a suitable fit

A

Induced fit model

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34
Q

In induced fit model enzymes lower the free _____ of the transition state by stabilizing the ______

A

Energy, transition state

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35
Q

It is a non protein organic substance which dialyzable and thermostable and loosely attached to the protein part

A

Coenzymes

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36
Q

An organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion

A

Prosthetic group

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37
Q

This include K+, Fe2+, Fe3+, Cu2+, Co2+, Zn2+, Mn2+, Mg2+, Ca2+ and Mo3+

A

Metal ion activator

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38
Q

An inactive enzyme is usually termed as _______ or ______

A

Zymogen, proenzymes

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39
Q

What are the activity that affect enzyme

A

Temperature
pH
Enzyme concentration
Substrate concentration
Covalent modification or phosphorylation or methylation
Inhibition
Allosteric effects

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40
Q

It is an inactive form

A

Proenzymes or zymogens

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41
Q

In order to activate this enzyme a small part of their polypeptide chain must be removed

A

Proenzyme (zymogens)

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42
Q

It is produced rather in its active form to avoid random reactions in body

A

Proenzyme or zymogens

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43
Q

In order to activate the proenzyme a ______ part of their _______ chain must be ________

A

Small, polypeptide, removed

44
Q

Proenzyme are produced rather in its ______form to avoid random reactions in the body

A

Active

45
Q

What are the examples of proenzyme or zymogens

A

Trypsinogen
Pepsinogen
Procaspase
Prolipase

46
Q

This regulation happens when substance binds to a certain part of the enzyme (but not on its active site) and changes the shape of its active site

A

Allosterism

47
Q

What do you call the enzyme that regulated in allosterism

A

Allosteric enzymes

48
Q

The substance that attaches to the allosteric enzyme is called a _____ and the site to which it binds is called the _____

A

Regulator, regulatory site

49
Q

A regulator that may inhibit the enzyme action

A

Negative modulation

50
Q

Regulator may stimulate the enzyme action

A

Positive modulation

51
Q

The attachment of the regulator to the enzyme is ______ and ______

A

Noncovalent, reversible

52
Q

What are the two kinetic states in allosteric enzyme

A

R form (relaxed form)
T form (taut form)

53
Q

A type of kinetic states that more active form of the enzyme

A

R form

54
Q

The kinetic state that is less active form of the enzyme

A

T form

55
Q

A ______ group is usually added to the apoenzyme changing the primary structure of the enzyme

A

Chemical

56
Q

Addition or removal of the chemical group may cause the ______ or ____ of an enzyme

A

Activation, inhibition

57
Q

Typical example of protein modification or covalent modification

A

Phosphorylation
Dephosphorylation

58
Q

Is the process of adding phosphate group

A

Phosphorylation

59
Q

An enzyme that catalyzes the breakdown of glycogen to glucose and is activated by addition of phosphate group

A

Glycogen phosphorylase

60
Q

The enzyme involved in glycogen synthesise is deactivated by the presence of phosphate groups

A

Glycogen synthase

61
Q

Is the removal of phosphate group

A

Dephosphorylation

62
Q

This type of modulation takes place when the same enzyme catalyzing the same substrate appear in different tissue but in different form

A

Isoenzyme

63
Q

What structure is formed when the same enzyme appears in different location with a different combination of subunits

A

Quaternary Structure

64
Q

_______ Allow very specific metabolic reactions to meet the particular needs of a given tissue or developmental stage

A

Isoenzyme

65
Q

What is the example of isoenzyme

A

Lactate dehydrogenase (LDH)

66
Q

What are the two isoenzyme in LDH

A

H4
M4

67
Q

The _____ isoenzyme is found in the heart

A

H4

68
Q

An isoenzyme that can be found in skeletal muscle

A

M4

69
Q

H4 isoenzymes functions in ______ condition

A

Aerobic

70
Q

M4 isoenzyme function in ______ condition

A

Anaerobic

71
Q

What are the different types of enzyme inhibitors

A

Reversible competitive inhibitor
Reversible non competitive inhibitor
Irreversible inhibitor
Uncompetitive inhibitor

72
Q

A molecule that has same shape and charge distribution as the enzyme substrates

A

Reversible competitive inhibitor

73
Q

It competes for occupancy at the binding site

A

Reversible competitive inhibitor

74
Q

When the inhibitor is attached to the enzyme no reaction occurs this results to the ______ in enzyme activity

A

Decrease

75
Q

When the complex breaks, the inhibitor _____ the active site. The enzyme is then _____ and ready to use

A

Leaves, free

76
Q

What competes for the active site

A

Substrate and inhibitor

77
Q

Increasing the substrate concentration will ______ the inhibitory effect

A

Decrease

78
Q

A molecule that binds the enzyme other than the active site

A

Reversible non competitive inhibitor

79
Q

Prevents the enzyme from performing its catalytic action

A

Reversible non competitive inhibitor

80
Q

Non-competitive inhibitor changes the ______ of the enzyme but not the ______

A

Confirmation, active site

81
Q

A molecule that forms strong covalent bond with the active site

A

Irreversible inhibitor

82
Q

Binds to the enzyme substrate complex but not to a free enzyme complex

A

Uncompetitive inhibitor

83
Q

They are generally activated by the substrate of the pathway and inhibited by the product of the pathway does allly turning the pathway on when it is needed

A

Allosteric regulation

84
Q

Allosteric regulation is also known as

A

Feedback inhibition

85
Q

Reversibly bind and dissociates from enzyme activity of enzyme recovered on removal of inhibitor usually non covalent in nature

A

Reversible inhibition

86
Q

The characteristic of an enzyme that is acts on the one and only one substance

A

Absolute specificity

87
Q

The characteristic of an enzyme that is acts on several structurally related substances

A

Relative specificity

88
Q

The characteristic of an enzyme that is able to distinguish between stereoisomers

A

Stereochemical specificity

89
Q

The substance that undergoes a chemical change catalyzed by an enzyme

A

Substrate

90
Q

A non protein molecule or ion required by an enzyme for catalytic activity

A

Cofactor

91
Q

An organic molecule required by enzyme for catalytic activity

A

Coenzyme

92
Q

A catalytically inactive protein formed by removal of cofactor from an active enzyme

A

Apoenzyme

93
Q

The location of an enzyme where a substrate is bound and catalysus occurs

A

Active site

94
Q

The rate at which an enzyme catalyzes a reaction

A

Enzyme activity

95
Q

The number of molecules of substrate acted on by one molecule of enzyme per minute

A

Turnover number

96
Q

A quantity of enzyme that catalyzes the conversion of 1 umol of substrate per minute under specified condition

A

Enzyme international unit (IU)

97
Q

The temperature at which enzyme activity is highest

A

Optimum temperature

98
Q

The ph at which enzyme activity is highest

A

Optimum pH

99
Q

A substance that decreases the activity of an enzyme

A

Enzyme inhibitor

100
Q

A substance that binds to an enzyme at allocation other than the active site and alters the catalytic activity

A

Modulator

101
Q

Allosteric enzyme has _____ structure whose activity is changed by the binding of ______

A

Quaternary, modulator

102
Q

A substance that binds to an allosteric enzyme and increases its activity

A

Activator

103
Q

A process in which the end product of a sequence of enzyme catalyzed reaction inhibits an earlier stop in the process

A

Feedback inhibition

104
Q

The synthesis of an enzyme in response to a cellular need

A

Enzyme induction

105
Q

pH optimum of pepsin

A

1-2 gastric

106
Q

pH optimum of trypsin

A

8-9 intestinal

Biochem Lec MID-TERMS (6 decks)

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