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610 Physical Sciences Of ANE > Chapter 19- Enzymes > Flashcards

Chapter 19- Enzymes Flashcards

1
Q

Proteins that catalyze biochemical reactions

A

Enzymes

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2
Q

Enzymes that catalyze oxidation-reeducation (redox)reactions

A

Oxidoreductase

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3
Q

An oxidoreductase enzyme that removes hydrogen from a molecule of lactate

A

Lactate dehydrogenase

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4
Q

T or F:other subclasses of the oxidoreductases include oxidases and reductases

A

T

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5
Q

Enzymes that catalyze the transfer of functional groups from one molecule to another

A

Transferases

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6
Q

An enzyme that catalyzes the transfer of an amino functional group

A

Transaminase

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7
Q

And enzyme that catalyzes the transfer of a methyl group

A

Transmethylase

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8
Q

An enzyme that catalyzes the transfer of a phosphorylation group

A

Kinase

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9
Q

What do kinases play a major role in

A

Energy harvesting processes involving ATP

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10
Q

An enzyme that catalyzes the transfer of a phosphorylation group from adenosine triphosphate (ATP) to a molecule of glucose in the first reaction of glycolysis

A

Hexokinase

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11
Q

An enzyme class that function through the addition of a water molecule to a bond, resulting in a bond breakage

A

Hydrolases

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12
Q

Class of enzymes important to the digestive system

A

Hydrolases

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13
Q

Catalyze the hydrolysis of glycosidic bonds between monosaccharides in a polysaccharide

A

Alpha- amylase

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14
Q

Catalyze the hydrolysis of peptide bonds in proteins to release amino acids

A

Proteases

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15
Q

Catalyze the hydrolysis of the ester bonds in triglycerides

A

Lipases

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16
Q

Class of enzymes that Catalyze the addition of a group to a double bond or the removal of a group to form a double bond

A

Lyases

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17
Q

Fumarase if an example of what class of enzymes

A

Lyases

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18
Q

What role does fumarase play in the citric acid cycle?

A

Catalyze the addition of a water molecule to the double bond of the substrate fumurate

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19
Q

What is the product that forms when fumarase catalyzes the addition of a water molecule to the double bond of the substrate fumurate?

A

Malate

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20
Q

Catalyzes the removal of an acetyl group from a molecule of citrate to form a double bond

A

Citrate lyase

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21
Q

What does ~ represent?

A

A high energy bond

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22
Q

What enzyme class is important in glycolysis

A

Isomerases

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23
Q

What enzyme group rearranges functional groups within a molecule and catalyze the conversion of one isomer into another

A

Isomerases

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24
Q

Converts one structural isomer, 3-phosphoglycerate, into another, 2-phosophoglycerate

A

Phosphoglycerate mutase

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25
Q

Phosphoglycreate mutase is in what class of enzymes

A

Isomerases

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26
Q

Class of enzymes that catalyze a reaction in which a C—C, C—S, C—O, or C—N bond is made or broken

A

Ligases

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27
Q

Catalyzes the joining of the hydroxyl group of a nucleotide in a DNA strand with the phosphorylation group of the adjacent nucleotide to form a phosphoester bond

A

DNA ligase

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28
Q

Common names for some enzymes are derived from the name of the ________

A

Substrate

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29
Q

The reactant that binds to the enzyme and is converted into product

A

Substrate

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30
Q

Molecules required by some enzymes to serve as donors or acceptors of electrons, hydrogen atoms, or other functional groups during a chemical reaction

A

Coenzymes

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31
Q

Transglutaminase is also known as

A

Meat glue

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32
Q

Belongs to a family of enzymes that catalyze a reaction between a glutamine residue in a protein and a lysine residue in the same or another protein

A

Transglutaminase

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33
Q

Factor _____ is essential for the formation of blood clots and is a Transglutaminase

A

XIII

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34
Q

How do you medically treat someone with Factor XIII deficiency

A

Give Transglutaminase

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35
Q

How does an enzyme speed up a chemical reaction?

A

Changes the path by which the reaction occurs, providing a lower energy route for the conversion of the substrate into the product—> AKA it lowers the activation energy

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36
Q

A reflection of the difference in energy between reactants and products

A

The Equillibrium constant equation

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37
Q

Why can an enzyme NOT alter the equilibrium constant for the reaction that is catalyzes?

A

The difference in energy between the reactants and the products is always the same

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38
Q

The threshold energy that must be overcome to produce a chemical reaction

A

Activation energy

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39
Q

T or F: as long as the substrate concentration increases , there is a direct decrease in the rate of the reaction

A

False… its a direct INCREASE in the rate of the reaction

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40
Q

T or F: the reaction rate of a reaction if independent of the amount of enzyme that is available

A

F: it is dependent on the amount of enzyme available

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41
Q

The part of the enzyme that binds with the substrate

A

The active site

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42
Q

With what forces does an enzyme attract and hold its substrate

A

Weak, noncovalent interactions—> hydrogen bonding, van der walls, dipole-dipole, electrostatic attractions

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43
Q

Who proposed the enzyme fit model we use today

A

‘Daniel E. Koshland

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44
Q

Model of enzyme activity that proposes that and active site of the enzyme is a flexible pocket that approximates and then molds to substrate shape (rather than it being a rigid model)

A

Induced fit model

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45
Q

The ability of the enzyme to bind to only one , or a very few, substrates

A

Enzyme specificity

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46
Q

The four classes of enzyme specificity

A
  1. Absolute specificity
  2. Group specificity
  3. Linkage specificity
  4. Stereochemical specificity
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47
Q

Type of enzyme specificity that catalyzes the reaction of only one substrate

A

Absolute specificity

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48
Q

Aminoacyl tRNA synthetases exhibit what type of specificity

A

Absolute

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49
Q

Type of specificity where an enzyme that catalyzes reactions involving similar molecules containing the same functional group

A

Group specificity

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50
Q

What type of specificity does hexokinase have

A

Group specificity

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51
Q

Type of specificity where an enzyme catalyzes the formation or breakage of only certain bonds in a molecule

A

Linkage specificity

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52
Q

Proteases, such as trypsin, chymotrypsin, and elastase are examples of what type of enzyme specificity

A

Linkage

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53
Q

Why are Proteases, such as trypsin, chymotrypsin, and elastases examples of linkage specificity

A

Selectively hydrolyze peptide bonds

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54
Q

An enzyme specificity that can distinguish one enantiomer from the other

A

Stereo chemical specificity

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55
Q

What type of specificity do most enzymes of the body exhibit

A

Stereochemical

56
Q

State in which the substrate is in an intermediate form, having features of both the substrate and the product

A

Transition state

57
Q

The _______state of an enzyme favors conversion of the substrate into product and release of the product

A

Transition

58
Q

The first protease inhibitor to be prescribed for pediatric AIDS patients

A

Nelfinavir

59
Q

Most recent HIV medication that is recommended for adults and adolescents

A

Darunavir

60
Q

In enzymes that require a non protein prosthetic group, the protein portion is called ___________ and the non protein group is called __________

A

Apoenzyme and cofactor

61
Q

The apoenzyme and cofactor together form the active enzyme called:

A

Holoenzyme

62
Q

Organic molecules that serve as carriers of electrons or chemical groups

A

Coenzymes

63
Q

True or false: coenzymes can only donate groups to the substrate, they cannot accept groups that are removed from the substrate

A

False: they can both donate and accept

64
Q

An organic substance that is required in the diet in small amounts

A

Vitamins

65
Q

The only water soluble vitamins acclimated with a coenzyme

A

Vitamin C

66
Q

NAD + and NADP+ are derived from what vitamin

A

Niacin

67
Q

FAD is made from what vitamin

A

Riboflavin

68
Q

Cytoplasm of the cell has a pH of

A

7.0

69
Q

The pH at which an enzyme functions optimally

A

PH optimum

70
Q

True or false: making a more basic or more acidic sharply decreases the rate of the reaction

A

True

71
Q

Why does a increase or decrease in pH decrease the rate of a reaction?

A

Alters the degree of ionization of amino acid R groups in the protein, as well as the extend to which they can hydrogen bond—> enzyme is denatured

72
Q

Optimum pH of pepsin

A

2.0

73
Q

A proteolytic enzyme in digestion that functions well in high pH environment

A

Trypsin

74
Q

Membrane bound vesicles containing about 50 different kinds of Hydrolases that degrade large biological molecules into small molecules

A

Lysosomes

75
Q

Optimal pH of lysosomal enzymes

A

4.8

76
Q

Explain protective mechanism of lysosomal membranes

A

Function optimally at pH of 4.8 and if they leak out of the lysosome or if a lysosome ruptures, the cytoplasmic pH of 7.0-7.3 renders them inactive

77
Q

Do enzymes in our cells remain stable at temps higher than 37 degrees Celsius or lower than that temp

A

Stable when lower than 37 degrees C

78
Q

At the ___________, the enzyme is functioning optimally and the rate of the reaction id maximal

A

Temperature optimum

79
Q

People with a genetic predisposition for familial emphysema have a genetic defect where

A

The gene that encodes the human plasma protein alpha 1-antitrypsin

80
Q

Allosteric means:

A

Other forms

81
Q

Why is enzyme activity controlled and regulated by the cell

A

To conserve energy

82
Q

A type of enzyme regulation that involves enzymes that have more than a single bonding site and they have active sites that can be altered by the binding of small molecules called effector molecules

A

Allosteric enzymes

83
Q

Effector binding converts the active site to an inactive configuration

A

Negative allosterism

84
Q

Effector binding converts the active site to an active configuration

A

Positive Allosterism

85
Q

__________ allosterism is an example of a feedback inhibition

A

Negative

86
Q

Allosteric enzymes are the basis for __________ of biochemical pathways

A

Feedback inhibition

87
Q

Feedback inhibition functions similar to a ________

A

Thermostat

88
Q

An enzyme in the inactive form

A

Proenzyme

89
Q

converts the proenzyme by __________ to the active form when it has reached the site of activity

A

Proteolysis

90
Q

Hydrolysis of a protein is called

A

Proteolysis

91
Q

Example of a proenzyme in digestion

A

Pepsinogen

92
Q

Another mechanism that the cell can use to turn an enzyme on or off— a process where chemical group is covalently added to or removed from the protein

A

Protein modification

93
Q

T or F: protein modification has only the capability to activate an enzyme, it cannot inactivate an enzyme

A

F: can activate and inactivate

94
Q

What is the most common type of protein modification

A

Phosphorylation or dephosporylation

95
Q

What is responsible for the covalent modification of an enzymes structure

A

It is catalyzed by other enzymes

96
Q

_________ add phosphorylation groups to a target enzyme, while _________ remove them

A

Protein kinases; phosphatases

97
Q

Give an example of phosphorylation inactivating an enzyme

A

Glycogen synthase

98
Q

T or F: in protein modification, an enzyme can be turned on or off in response to environmental or physiological conditions

A

T

99
Q

Chemicals that bind to enzymes and wither eliminate or drastically reduce their catalytic activity

A

Enzyme inhibitors

100
Q

What is a medical example of an enzyme inhibitor

A

Penicillin

101
Q

How are enzyme inhibitors classified

A

Reversible vs irreversible and competitive vs non competitive

102
Q

Arsenic is what class of enzyme inhibitors

A

Irreversible inhibitors

103
Q

Class of enzyme inhibitors that bind very tightly, something’s even covalently, to the enzyme

A

Irreversible inhibitors

104
Q

Give two examples of irreversible inhibitor enzymes

A

Snake venom and nerve gases

105
Q

What are reversible, competitive enzymes often called

A

Structural analogs

106
Q

Molecules that resemble the structure and charge distribution of the natural substrate for a particular enzyme

A

Reversible, competitive enzyme inhibitors

107
Q

Antidote for poisoning by organophosphates

A

PAM—> pyridine aldoxime methiodide

108
Q

Sulfa drugs are examples of what kind of enzyme inhibitor

A

Competitive inhibitors

109
Q

A vitamin required for the transfer of methyl groups in biosynthesis of methionine and the nitrogenous bases required to make DNA and RNA

A

Folic Acid

110
Q

The substrate foe an early step in folic acid synthesis

A

PABA—> para-aminobenzoic acid

111
Q

Break the peptide bonds that maintain the primary protein structure

A

Proteolytic enzymes

112
Q

An enzyme that hydrolyzes dietary proteins in the small intestine

A

Chymotrypsin

113
Q

Does chymotrypsin act on the amino or carbonyl side of a peptide bond

A

Carbonyl

114
Q

The pancreatic serine proteases trypsin, chymotrypsin, and elastase all hydrolyze what

A

Peptide bonds

115
Q

Where are trypsin, chymotrypsin, and elastase produced and transported

A

Produced in pancreas and transported to small intestine

116
Q

Why are trypsin, chymotrypsin, and elastase called serine proteases?

A

They have amino acid serine in the catalytic region of the active site that is essential for hydrolysis of the peptide bond

117
Q

A pancreatic serine protease that cleaves peptide bonds on the carbonyl side of the aromatic amino acids and large, hydrophobic amino acids such as methionine

A

Chymotrypsin

118
Q

A pancreatic serine protease that cleaves peptide bonds on the carbonyl side of basic amino acids

A

Trypsin

119
Q

A pancreatic serine protease that cleaves peptide bonds on the carbonyl side of glycine and alanine

A

Elastase

120
Q

3 primary tools used to assess cardiac injury

A

Myoglobin, creatine kinase-MB (CK-MB), and cardiac troponin I

121
Q

Most reliable test *due to it being cardiac specific)for cardiac injury supported by American college of cardiology

A

Troponin

122
Q

What is the first cardiac bio marker to appear in a cardiac injury and why

A

Myoglobin, small and diffuses rapidly

123
Q

Myoglobin is rapidly cleared from body by kidneys in about how many hours

A

16-36 h

124
Q

When do CK-MB levels usually return to normal

A

48-72 hours

125
Q

Med used in Cardiac procedure to break apart thrombus in coronary vessel and inhibit thrombin

A

Streptokinase

126
Q

TPA converts the proenzyme, _______, into the active enzyme, __________

A

Plasminogen, plasmin

127
Q

Elevation in what two enzymes indicate pancreatitis

A

Amylase and lipase

128
Q

if ALT elevation is > AST elevation, is the issue liver or heart

A

Liver

129
Q

A genetic disorder resulting in the deficiency of the enzyme glucocerebrosidase—> leads to buildup of glucocerebroside in liver spleen and bone marrow causing excess lipid in these places. Causes severe anemia, thrombocytopenia, and hepatosplenomegaly, and skeletal problems

A

Gaucher’s disease

130
Q

What is treatment for Gauchers and what does it do

A

Cerezyme—> hydrolyzes glucocerebroside into glucose and ceramide so products can be metabolized normally

131
Q

What would happen to the rate of an enzyme catalyzed reaction if pH was increased from 7 to 12

A

Will cause decrease in rate… most enzymes denature at pH of 11 and enzyme activity would cease

132
Q

Why do extremes of pH inactivate enzymes

A

Can cause an enzyme to become polyanionic or polycationic which could lead to denaturing and loss of enzyme activity . Less drastic changes in ph alter r group active site which destroys enzyme activity

133
Q

Where is pepsin formed

A

Stomach

134
Q

Where is trypsin formed

A

Pancreas

135
Q

T or F: the reaction rate is dependent on the amount of substrate that is available

A

F… dependent on amount of enzyme

610 Physical Sciences Of ANE (5 decks)

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