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BioChem for MedTech > Enzymes > Flashcards

Enzymes Flashcards

1
Q

It is a compound usually a protein, that acts as a

catalyst for a biochemical reaction

A

Enzyme

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2
Q

Composed only of protein

A

Simple Enzyme

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3
Q

Has a non protein part in addition to a protein part.

A

Conjugated Enzyme

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4
Q

Protein of the conjugated enzyme

A

Apoenzyme

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5
Q

Non protein part of the conjugated enzyme

A

Cofactor

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6
Q

Biochemically active conjugated enzyme produced from an

apoenzyme and a cofactor

A

Holoenzyme

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7
Q

Serves as a cofactor in a conjugated enzyme

A

Coenzyme

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8
Q

Reactant in an enzyme catalyzed reaction.

A

Substrate

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9
Q

Requires a coenzyme that is oxidized or reduced as the

substrate is reduced or oxidized

A

Oxidoreductase

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10
Q

Catalyzes the transfer of a functional group from one

molecule to another

A

Transferase

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11
Q

Catalyzes the transfer of amino group from one molecule to another

A

Transaminase

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12
Q

Catalyzes the transfer of phosphate group from ATP to give ADP and
a phosphorylated product.

A

Kinases

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13
Q

Catalyzes the hydrolysis reaction and is the central to the process of digestion

A

Hydrolase

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14
Q

Catalyzes the addition of a group to a double bond or the
removal of a group to form a double bond in a manner
that does not involve hydrolysis or oxidation

A

Lyase

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15
Q

Catalyzes the isomerisation of a substrate in a reaction

converting it to a molecule isomeric with itself.

A

Isomerase

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16
Q

Catalyzes the bonding together of two molecules into

one with the participation of ATP.

A

Ligase

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17
Q

Small part of an enzyme’s structure that is actually

involved in catalysis.

A

Active Site

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18
Q

The intermediate reaction species that is formed when a

substrate binds to the active site of an enzyme.

A

Enzyme-Substrate Complex

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19
Q

Active site in the enzyme has the fixed, rigid

geometrical conformation.

A

Lock-and-Key Model

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20
Q

Enzyme’s active site is not rigid and static.

A

Induced-Fit Model

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21
Q

Extent to which an enzyme’s activity is restricted to a
specific substrate, a specific group of substrate, a
specific type of chemical bond, or a specific type of
chemical reaction.

A

Enzyme Specificity

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22
Q

Catalyze only one reaction

A

Absolute Specificity

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23
Q

Act only on molecules that have a specific functional

group, such a hydroxyl, amino or phosphate groups.

A

Group Specificity

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24
Q

A caboxylpeptidase is an example of what specificity?

A

Group Specificity

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25
Q

A Catalase is an enzyme of what specificity?

A

Absolute Specificity

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26
Q

Act on the particular type of bond, irrespective to the

rest of the molecular structure.

A

Linkage Specificity

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27
Q

Act on a particular isomer

A

Stereochemical Specificity

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28
Q

Measures the rate at which an enzyme converts

substrate to products in a biochemical reaction

A

Enzyme Activity

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29
Q

Factors that affect the enzyme activity are:

A

Temperature
pH
Substrate Concentration
Enzyme Concentration

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30
Q

Temperature at which an enzyme exhibits maximum activity

A

Optimum Temperature

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31
Q

the charge on acidic and basic amino acids located at the active site
depends on?

A

pH

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32
Q

What can affect substrate, causing either protonation or

deprotonation of groups on the substrate.

A

pH

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33
Q

Active in the stomach, functions best at pH 2.0

A

Pepsin

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34
Q

Operates in the small intestines, function best at pH 8.0

A

Trypsin

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35
Q

physiological pH ranges from?

A

7.0-7.5

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36
Q

True or False
Decreased concentration of substrate will obtain the
enzyme activity.

A

False

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37
Q

Number of substrate molecules transformed per minute by
one molecule of enzyme uunder optimum conditions of
temperature, pH and saturation.

A

Turnover Number

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38
Q

True or False
The greater the enzyme concentration, the lesser the
reaction rate.

A

False

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39
Q

A microbial enzyme active at a conditions that would inactivate
human enzymes as well as enzymes present in other types of
higher organisms

A

Extremozymes

40
Q

Microorganisms that thrives in extreme environments

A

Extremophile

41
Q

Microorganisms with optimal growth at pH levels of 3.0 or below

A

Acidophile

42
Q

Microorganisms with optimal growth at pH levels of 9.0 or above

A

Alkaliphile

43
Q

Microorganisms whose temperature between 80C and 122C are needed to thrive

A

Hyperthermophile

44
Q 
Substance that slows or stops the normal catalytic
function of an enzyme by binding to it.
A

Enzyme Inhibitor

45
Q

Molecule that sufficiently resembles an enzyme substrate in
shape and charge distribution that it can compete with the
substrate for occupancy of the enzymes active site

A

Competitive Enzyme Inhibitor

46
Q

Molecule that decreases enzyme activity by binding to a site
on an enzyme other than the active site. Presence of this causes a change in the structure of the
enzyme sufficient to prevent the catalytic groups at the active
site from properly effecting their catalyzing action.

A

Non-competitive Enzyme Inhibitor

47
Q

Molecule that inactivates enzyme by forming a strong
covalent bond to an amino acid side chain group at the
enzymes active site.
Do not have structures similar to that of the enzyme’s normal
substrate.

A

Irreversible Enzyme Inhibitor

48
Q

True or False
A cell that continually produces large amount of
enzyme for which substrate concentration is always
high is wasting energy. The production of the
enzyme needs to be “ turned off”.

A

False, substrate concentration is always “very low”

49
Q

True of False
A product of an enzyme Catalyzed reaction that is
present in plentiful amounts in a cell is a waste of
energy if the enzyme stopped catalyzing the
reaction that produces the product. The enzyme needs
to be turned off.

A

False, if the enzyme “continues to catalyze”

50
Q

Substance that bind at the regulatory sites of allosteric

enzymes.

A

Regulators

51
Q

The shape of the active site is changed such that it

can more readily accept substrate.

A

Positive Allosteric Regulators

52
Q

Changes to the active site are such that substrate is

less readily accepted.

A

Negative Allosteric Regulators

53
Q

A process in which activation or inhibition of the first
reaction in a reaction sequence is controlled by a
product of reaction sequence.

A

Feedback Control

54
Q

Catalyzes the breaking of peptide bonds that maintain the

primary structure of protein.

A

Proteolytic Enzymes

55
Q

Inactive precursor of a proteolytic enzyme.

A

Zymogens

56
Q

Process in which enzyme activity is altered by
covalently modifying the structure of the enzyme
through attachment of a chemical group or removal of
a chemical group from a particular amino acid within
the enzyme structure.

A

Covalent Modification

57
Q

Process of addition of the phosphate group to the

enzyme by protein kinases

A

Phosphorylation

58
Q

Removal of the phosphate group from the enzyme by

phosphatases

A

Dephosphorylation

59
Q

is an enzyme with two or more protein chains (quaternary

structure) and two kinds of binding sites (substrate and regulator).

A

Allosteric Enzyme

60
Q

an enzyme involved in the breakdown of glycogen to glucose

A

Glycogen phosphorylase

61
Q

catalyze removal

of the phosphate groups.

A

Phosphatases

62
Q

An enzyme that which effect the addition of phosphate groups

A

Protein kinases

63
Q

is a substance that kills bacteria or inhibits their growth.

A

Antibiotic

64
Q

An inhibitor that decreases enzyme activity by binding to a site on the enzyme other
than the active site

A

Reversible noncompetitive inhibitor

65
Q

An inhibitor that inactivates enzymes by forming a strong covalent bond at the enzyme
active site

A

Irreversible Inhibitor

66
Q

An inhibitor that has a shape and charge distribution similar to that of the enzyme’s
normal substrate

A

Reversible competitive inhibitor

67
Q

An inhibitor whose effect can be reduced by simply increasing the concentrate of
normal substrate present

A

Reversible competitive inhibitor

68
Q

A molecule closely resembling the
substrate. Binds to the active site and
temporarily prevents substrates from
occupying it, thus blocking the reaction

A

Competitive Enzyme Inhibitor

69
Q 
A molecule that binds to a site on an
enzyme that is not the active site. The
normal substrate still occupies the active
site but the enzyme cannot catalyze the
reaction due to the presence of the
inhibitor.
A

Noncompetitive Enzyme Inhibitor

70
Q

A molecule that forms a covalent bond to
a part of the active site, permanently
preventing substrates from occupying it.

A

Irreversible Enzyme Inhibitor

71
Q

The active site has a fixed geometric
shape. Only a substrate with a matching
shape can fit into it.

A

Lock-and-Key Model

72
Q 
The active site has a flexible shape
that can change to accept a variety of
related substrates. Enzymes vary in
their degree of specificity
for substrates.
A

Induced-Fit Model

73
Q

Such specifi city means an enzyme will catalyze a particular
reaction for only one substrate. This most restrictive of all specifi cities is not
common. Urease is an enzyme with absolute specificity.

A

Absolute Specificity

74
Q

Such specificity means an enzyme can distinguish between
stereoisomers. Chirality is inherent in an active site, because amino acids are chiral
compounds. L-Amino-acid oxidase will catalyze reactions of L-amino acids but not
of D-amino acids.

A

Stereochemical Specificity

75
Q

Such specificity involves structurally similar compounds that have
the same functional groups. Carboxypeptidase is group-specifi c; it cleaves amino
acids, one at a time, from the carboxyl end of the peptide chain.

A

Group Specificity

76
Q

Such specificity involves a particular type of bond, irrespective of
the structural features in the vicinity of the bond. Phosphatases hydrolyze phosphate–
ester bonds in all types of phosphate esters. Linkage specifi city is the most general of
the specifi cities considered.

A

Linkage Specificity

77
Q

is the intermediate reaction species that is formed when a

substrate binds to the active site of an enzyme.

A

Enzyme-substrate complex

78
Q

is the relatively small part of an enzyme’s structure that is actually involved in catalysis.

A

Active Site

79
Q

introduction of double bond (oxidation)
by formal removal of two H atoms from
substrate, the H being accepted by a
coenzyme

A

Dehydrogenase

80
Q

transfer of an amino group between

substrates

A

Transaminases

81
Q

transfer of a phosphate group between

substrates

A

Kinases

82
Q

hydrolysis of ester linkages in lipids

A

Lipase

83
Q

hydrolysis of amide linkages in

proteins

A

Protease

84
Q

hydrolysis of sugar–phosphate ester

bonds in nucleic acids

A

Nuclease

85
Q

hydrolysis of glycosidic bonds in

carbohydrates

A

Carbohydrase

86
Q

hydrolysis of phosphate–ester bonds

A

Phosphatase

87
Q

removal of H2O from substrate

A

Dehydratase

88
Q

removal of CO2 from substrate

A

Decarboxylase

89
Q

removal of NH3 from substrate

A

Deaminase

90
Q

addition of H2O to a substrate

A

Hydratase

91
Q

conversion of D to L isomer, or vice

versa

A

Racemase

92
Q

transfer of a functional group from
one position to another in the same
molecule

A

Mutase

93
Q

formation of new bond between two

substrates, with participation of ATP

A

Synthetase

94
Q

formation of new bond between a
substrate and CO2, with participation
of ATP

A

Carboxylase

95
Q

an enzyme that catalyzes the formation of peptide

cross links between polysaccharide strands in bacterial cell walls.

A

Transpeptidase

96
Q

is an organic compound, essential in small amounts for the proper
functioning of the human body, that must be obtained from dietary sources because the
body cannot synthesize it.

A

Vitamin

BioChem for MedTech (3 decks)

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