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Biochemistry Lecture > ENZYMES > Flashcards

ENZYMES Flashcards

1
Q

• Papain/Papase

A

From papaya

fruit enzyme

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2
Q

• Bromelain

A

Pineapple
Used as meat tenderizer
Used for constipation

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3
Q

• Peptidase

A

cleaves polypeptide chains

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4
Q

• Proteolytic enzymes

A

Cleaves proteins in general

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5
Q

• Salivary Amylase

A

Digestion of starch

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6
Q

• Digestive enzymes

A

Chymotrypsin
Trypsin
Pepsin

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7
Q

pH of digestive enzynes

A

pH 2

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8
Q

Brain enzymes

A

Acetylcholinesterase

Monoamine oxidase

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9
Q

Liver enzymes

A 
Alanine aminotransferase (ALT)
Aspartate aminotransferase (AST)
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10
Q

Glucose-6 Phosphate Dehydrogenase

A

involved in glucose metabolism – glycolysis

part of newborn screening

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11
Q

Lactase

A

Breakdown of Lactose

Inadequacy leads to lactose intolerance meaning cannot breakdown lactose (milk) leading to diarrhea

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12
Q

Alcohol dehydrogenase and Aldehyde dehydrogenase

A

Detoxification of alcohol
Converts acetaldehyde to ethanol
Inadequacy can lead to low alcohol tolerance

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13
Q

Decarboxylase

A

Catalyzed decarboxylation

Decarboxylation is the chemical reaction involved in removal of carboxyl group while releasing carbon dioxide

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14
Q

Cardiac enzymes

A

Troponin and Creating Phosphokinase (CPK)

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15
Q

Lipase

A

breakdown of lipids

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16
Q

Antioxidant enzymes

A

Glutathione peroxidase
Glutathione reductase
Catalase

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17
Q

Catalase

A

Breakdown and detoxification of hydrogen peroxide (H2O2)

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18
Q

o protein part of an enzyme

A

apoenzyme

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19
Q

o non-protein portion of an enzyme that is necessary for catalytic function

A

• Cofactor

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20
Q

Examples of cofactors

A

Zn2+ and Mg2+ (inorganic compounds)

Without this cofactor will not make the enzyme functional

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21
Q

o non-protein organic molecule, frequently a B-vitamin, that acts as a cofactor
o on a different level
Energy-rich compounds

A

coenzyme

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22
Q

o compound/s whose reaction an enzyme catalyzes

A

• Substrate

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23
Q

o specific portion of the enzyme to which a substrate binds during reaction

A

Active site

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24
Q

Crevice or cleft of an enzyme

A

• Active site

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25
Q

site of reaction

A

Active site

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26
Q

any process that initiates or increases the activity of an enzyme

A

Activation

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27
Q

portion on the enzyme surface where inhibitors/activators bind to regulate catalytic reactions

A

Allosteric site

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28
Q

o where inhibitors can compete with the substrate to activate and regulate catalytic reactions

A

Allosteric site

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29
Q

compound/s that slows down the rate of the reaction

A

Inhibitors

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30
Q

process that makes an active enzyme less active or inactive

A

• Inhibition

Mechanism of Drugs

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31
Q

Enzyme Catalysis

A

Substrate-specific (stereoselective , site targeting)
Efficient
Enzyme Specificity
Reaction Specificity

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32
Q

o the ability of an enzyme to discriminate among possible substrate molecules

A

Enzyme specificity

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33
Q

o Highly specific for reactants/substrates SIZE AND SHAPE can mediate a chemical reaction.

A

Reaction specificity

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34
Q

 Conformation or confirmation based on the presence of a particular amino acid.
 Concepts of R groups, polarity, hydrophobicity

A

 Stereoselective

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35
Q

 Important because the active part of the enzyme is the active site.
 Presence of inhibitors

A

 Site targeting

36
Q

o Can accelerate a reaction (109 - 1020)

A

Efficient

37
Q

molecular species consisting of a substrate (S) bound to the active site of an enzyme (E)

A

Enzyme-substrate (ES) complex

38
Q

Two scenarios in ES complex

A

Easy Fit

Enzyme would need to adjust

39
Q

Transient product is formed if

A

during the scenario that enzyme slightly adjusted

transient - sandali lang

40
Q

Transition state

A

when the activation energy has been OVERCOME and the products are formed leaving the active site of an enzyme

41
Q

REMEMBER THAT

role of enzyme on formation of product

A

the enzyme does not participate thermodynamically in the formation of the product.

It just simply hastens the formation of product in the active site of the enzyme.

with that the enzyme CAN STILL BE RECOVERED

Doe NOT affect final product. it only acts as ACCELERATOR

42
Q

Role of trypsin

A

Catalyzes the hydrolysis of peptide bonds formed by the carboxyl group of LYSINE and ARGININE

43
Q

• The intermediate compound formed from the combining of catalysts with the substrate

A

Enzyme-substrate complex

44
Q

Binding of the active site occurs through

A

NON-COVALENT INTERACTION

45
Q

o Enzymes speed up a reaction by

A

LOWERING THE ACTIVATION ENERGY of a given reaction

the enzyme will help primarily the substate and enzyme to attain a transition state

46
Q

rate of appearance of products or rate of disappearance of substrate

A

• Rate of a chemical reaction

47
Q

(highest
point on an energy diagram of a
reaction)

A

Transition state

48
Q

the necessary
amount of energy and the correct
arrangement of atoms to produce
products

highest amount of
energy required and there should be a
correct arrangement of atoms to produce
a product

A

Transition state

49
Q

the amount of energy inputted and is
computed based on the exponent on the
rate equation

A

Order of reaction

50
Q

– reaction that
proceeds at a constant rate and is
independent of reactant

A

Zero order

51
Q

rate reacts on the
first power of the concentration of
a single reaction

A

First order

52
Q

rate is
proportional to the products of the
concentration of the two reactants

A

Second order

53
Q

No adjustments can be made in the conformation

A

Lock and key model mechanism

54
Q

Active site becomes modified to accommodate the substrate

A

Induced fit model

55
Q 
Assumes small (minor) but continuous changes in the active
site structures
A

Induced fit mode

56
Q

active site is a rigid, inflexible 3D body

A

Lock and key model mechanism

57
Q

Type of inhibitor: assembles the structure of normal substrate
and it’s capable of binding to the active site of the
enzyme

A

Competitive

58
Q

Type of inhibitor: both the inhibitor and substrate can bind

simultaneously to two different sites on the enzyme

A

Noncompetitive

59
Q

Type of inhibitor: allow substrate to bind the active site and or binds
only to the ES complex and not with the free
enzyme; thus, influencing the activity of the enzyme
only when the substrate concentration and, in turn,
ES concentration are high

A

Uncompetitive

60
Q

Type of inhibitor: there is another site other than the active site that
the substrate can bind to and as well as inhibitor

A

Noncompetitive

61
Q

Type of inhibitor: follows allosterism

A

Noncompetitive

62
Q

an efficient
enzyme control mechanism because the entire series of
reactions can be shut down, when an excess of the final
product exists, thus preventing the accumulation of the
intermediary products (called intermediates) in the
pathway or sequence of reaction

A

Enzyme Regulation

63
Q

What are the enzyme regulations

A

Feedback control
Proenzyme (Zymogen)
Allosterism

64
Q

Also known as Feedback inhibition / End product

inhibition

A

Feedback control

65
Q

An enzyme-regulation process where the product of a
series of enzyme-catalyzed reactions inhibits an earlier
reaction in the sequence.

A

Feedback control

66
Q

Enzyme regulation wherein

The inhibition may be competitive or noncompetitive.

A

Feedback control

67
Q

An inactive form of an enzyme that must have part of its
polypeptide chain hydrolyzed and removed before it
becomes active.

A

Proenzyme / Zymogen

68
Q

Digestive enzymes / proteolytic enzymes that are initially produced as
zymogen

A

Trypsin / Trypsinogen
Chymotrypsin / chymotrypsinogen

It becomes active only after a six amino acid
fragment is hydrolyzed and removed from the end
terminal end of its chain. In so doing, removal of these
small fragments changes not only the primary structure,
but also the tertiary structure, allowing the molecule to
achieve its active form.

69
Q

Type of inhibition that has NO CATALYTIC REACTION

A

Noncompetitive

70
Q

Enzyme regulation based on an event occurring at a place
other than the active site but that creates a change in the
active site

A

Allosterism

71
Q

An enzyme regulated by allosterism is called an

A

allosteric enzyme

72
Q

Inhibition of an allosteric

enzyme

A

Negative modulation

73
Q

Stimulation of an allosteric

enzyme.

A

Positive modulation

74
Q

Process of affecting enzyme activity by COVALENTLY MODIFYING it

A

Protein modification

75
Q

Causes a change in the primary structure through the
addition of a functional group covalently bound to the
apoenzyme

A

Protein modification

76
Q

Enzyme that occurs in multiple forms that each catalyzes the

same reaction

A

ISOZYMES/ ISOENZYMES

77
Q

• A molecule whose shape mimics the transition state of s

substrate

A

Transition state analogs

78
Q

When they mimic, they can now be used as enzyme

inhibitors.

A

Transition state analogs

79
Q

An antibody that has catalytic activity because it was

created using a transition state analog as an immunogen

A

Abzymes

80
Q

This is the principle in making designer enzymes by
biotechnology molecular technology then you’ll be able
to prepare or make designer enzymes to be able to
catalyze various types or a wide variety of reactions

A

TRansition state analog (Abzymes?)

81
Q

• Series of mathematical relationship that explains the

behavior of non-allosteric enzymes

A

Michaelis Menton Equation

82
Q

Combination of zero order and 1st order kinetics

A

Michaelis Menton Equation

When S is low, the equation for rate is 1st order in S
• When S is high, the equation for rate is 0-order in S

83
Q

describes the velocity of enzymes
catalyst reaction where there is saturating
level of the substrate

A

V max:
v max can be used to
determine the individual rate
constant but to a certain extent

84
Q

What is KM

A

Michaelis constant

85
Q

it is mathematically equal to the substrate
concentration that generates half of the
maximum velocity

A

Michaelis constant (KM)

86
Q

Disadvantage of Michaelis-menton equation

A

you will be able to calculate now the velocity
given the substrate concentration but only to a certain
extent because there is a saturation point

87
Q

The curve is hyperbolic compared to other graphs
which are sigmoidal. So it gives you a rectangular
hyperbolic dependency curve of the velocity on the
substrate

A

Michaelis constant equation

Biochemistry Lecture (8 decks)

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