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Biochemistry > Enzymes > Flashcards

Enzymes Flashcards

1
Q
  • proteins that catalyze the biochemical reactions
  • 6 classes based on the type of reaction they catalyze
A

enzymes

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2
Q

it would tend to be slow or not happen at all

A

uncatalyzed reactions

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3
Q

catalyze the oxidation-reduction (redox) reactions

A

oxidoreductases

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4
Q

removes hydrogen from a molecule of lactae

A

lactase dehydrogenase

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5
Q

catalyze the transfer of functional groups from one molecule to another

A

transferases

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6
Q

transfer of an amino functional group

A

Transaminase

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7
Q

transfer of a methyl group

A

Transmethylase

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8
Q
  • transfer of a phosphoryl group
  • major role in energy-harvesting processes involving ATP
A

kinase

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9
Q

transfer of a phosphoryl group from adenosine triphosphate (ATP) to a molecule of glucose

A

hexokinase

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10
Q
  • catalyze hydrolysis reactions
  • important in the digestive process
A

hydrolases

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11
Q
  • hydrolysis of glycosidic bonds between monosaccharides in a polysaccharide
  • ex. α-amylase
A

gylcosidases

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12
Q

hydrolysis of peptide bonds in proteins to release amino acids

A

proteases

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13
Q

hydrolysis of the ester bonds in triglycerides

A

lipases

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14
Q
  • catalyze the addition of a group to a double bond
  • catalyze the removal of a group to form a double bond
A

lyases

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15
Q

citric acid cycle

A

fumarase

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16
Q
  • addition of a water molecule to the double bond of the substrate fumarate
A

citric acid cycle

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17
Q
  • removal of a group and formation of a double bond
  • catalyzes the removal of an acetyl group from a molecule of citrate
A

citrate lyase

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18
Q
  • rearrange the functional groups within a molecule
  • catalyze the conversion of one isomer into another
A

isomerases

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19
Q

products of citrate lyase

A
  • oxaloacetate
  • acetyl CoA
  • ADP
  • inorganic phosphate group (Pi)
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20
Q
  • rates double when substrate concentration is doubled
  • substrate concentration increases = direct increase in the rate of the reaction
A

uncatalyzed chemical reactions

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21
Q
  • part of the enzyme that binds with the substrate
  • conformation of the active site determines the specificity of the enzyme
A

active site

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22
Q

made up of amino acid R groups involved in substrate binding, and not necessarily catalysis

A

binding site

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23
Q
  • Emil Fischer (1984)
  • substrate simply snapped into place like a piece of a jigsaw puzzle or a key into a lock
A

lock and key model

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24
Q
  • Daniel E. Koshland (1985)
  • proteins are flexible molecules
A

induced fit model

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25
Q

tightly wound in structures in the nucleus of the cell

A

chromosomes

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26
Q

one of the first to study genetics in a systematic way

A

gregor model

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27
Q
  • substance in the nuclei of white blood cells
  • 14% nitrogen and 3% phosphorus in addition to carbon, hydrogen, and oxygen
A

nuclein

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28
Q

nuclein is now called as?

A

deoxyribonucleic acid

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29
Q
  • critical role in the process of cell division
  • composed of both protein and nuclein
A

chromosomes

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30
Q

polymers of 20 different amino acids

A

proteins

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31
Q

polymers of 4 sub-units

A

nuclein

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32
Q
  • carries all of the genetic information
  • sugar 2’-deoxyribose
A

DNA

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33
Q
  • responsible for interpreting the genetic information into proteins
  • sugar ribose
A

RNA

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34
Q

what are the pyrimidines in DNA

A

cytosine and thymine

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35
Q

what are the pyrimidines in RNA

A

cytosine and uracil

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36
Q

what are the purines found in both dna and rna

A

adenine and guanine

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37
Q

ribonucleosides formed from cytosine

A

cytidine

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38
Q

ribonucleosides formed from uracil

A

uridine

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39
Q

purines - nucleosides formed with ribose and adenine

A

adenosine

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40
Q

purines -nucleosides formed with ribose and guanine

A

guanosine

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41
Q
  • selectively hydrolyze peptide bonds
  • ex. trypsin, chymotrypsin, and elastase
A

proteases

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42
Q

active enzyme formed by the apoenzyme and cofactor

A

holoenzyme

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43
Q

only water-soluble vitamin that has not been associated with a coenzyme

A

vitamin C

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44
Q
  • negative allosteric effector of phosphofructokinase
  • inhibits the activity of phosphofructokinase
A

ATP

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45
Q

production of the enzyme in an inactive form

A

froenzymes

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46
Q

froenzymes are converted to ___ to the active form when it has reached the site of its activity

A

proteolysis

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47
Q

inhibits several enzymes that are involved in the synthesis of bacterial cell walls

A

Penicilin

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48
Q

chemicals that can bind to enzymes and either eliminate or drastically reduce their catalytic ability

A

Enzyme inhibitors

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49
Q

vitamin that is found in sulfa drugs and required for the transfer of methyl groups in the biosynthesis of methionine and the nitrogenous bases required to make DNA and RNA

A

Folic acid

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50
Q
  • enzyme that hydrolyzes dietary proteins in the small intestine
  • acts specifically on the carbonyl side of the peptide bond
A

Chymotrypsin

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51
Q

lack of blood supply

A

Ichemia

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52
Q

catalyzes the production of the proteolytic enzyme plasmin from plasminogen

A

Streptokinase

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53
Q

proenzyme

A

plasminogen

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54
Q
  • degrade a fibrin clot into subunits
  • dissolve the clot
  • subunits inhibit further clot formation by inhibiting thrombin
A

plasmin

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55
Q
  • inflammation of the pancreas
  • elevated blood serum concentrations of the enzymes amylase and lipase
A

Pancreatitis

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56
Q

what are some liver diseases

A

cirrhosis and hepatitis

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57
Q

structure wherein the supercoiled DNA molecule is attached to a complex of proteins at roughly 40 sites along its length, forming a series of loops

A

Nuceloid

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58
Q
  • extra chromosome 13
  • extremely rare
  • extreme mental and physical defects and early death
A

Patau syndrome

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59
Q
  • additional chromosome 18
  • extremely rare
  • extreme mental and physical defects and early death
A

Edward syndrome

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60
Q
  • males with two X chromosomes and one Y
  • sexual immaturity and breast development
A

Klinefelter syndrome

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61
Q
  • woman with only a single X chromosome
  • short stature, a webbed neck, and sexual immaturity
A

Turner syndrome

62
Q

essential that produces an absolutely accurate copy of the original genetic information

A

DNA replication

63
Q

DNA replication begins at a unique sequence on the circular chromosome

A

Replication origin

64
Q
  • point at which the new deoxyribonucleotide is added to the growing daughter strand
  • DNA has been opened to allow binding of the various proteins and enzymes responsible for DNA replication
A

Replication fork

65
Q
  • replication occurs bidirectionally at the rate of about 500 new nucleotides every second
  • two replication forks moving in opposite directions
A

Bidirectional

66
Q

break the hydrogen bonds between the base pairs

A

Helicase

67
Q
  • alleviates positive supercoiling
  • travels along the DNA ahead of the replication fork
A

Topoisomerase

68
Q

binds to the separated strands, preventing them from coming back together

A

single-strand binding protein

69
Q
  • “reads” each parental strand or “template”
  • catalyzes the polymerization of a complementary daughter strand
A

DNA polymerase III

70
Q
  • replicated discontinuously
  • many RNA primers are produced as the replication fork proceeds along the molecule
A

Lagging strand

71
Q
  • DNA polymerase III catalyzes DNA chain elongation from each of these primers
  • new strand “bumps” into a previous one, synthesis stops at that site
A

Lagging strand

72
Q

formed by the three nucleotides at the base of the cloverleaf structure

A

anticodon

73
Q

assists the recognition of the splice boundaries and stabilization of the splicing complex

A

spliceosomes

74
Q

addition of a water molecule to a bond, resulting in bond breakage

A

hydrolases

75
Q

what cycle has a addition of a water molecule to the double bond of the substrate fumarate

A

citric acid cycle

76
Q

rearrange the functional groups within a molecule and catalyze the conversion of one isomer into another

A

isomerases

77
Q

it catalyze a reaction in which C-C, C-S, C-O, or C-N bond is made or broken

A

ligases

78
Q

it is joining of the hydroxyl group of a nucleotide in a DNA strand with the phosphoryl group of the adjacent nucleotide to form a phosphoester bond

A

DNA ligase

79
Q

what catalyzes the hydrolysis of urea

A

urease

80
Q

what catalyzes the hydrolysis of lactose

A

lactase

81
Q

what reaction is the removal of hydrogen atoms from a substrate

A

dehydrogenases

82
Q

what reaction is the addition of hydrogen atoms to a substrate

A

decarboxylases

83
Q

what reaction is the addition of carboxyl groups to a substrate

A

carboxylases

84
Q

every chemical reaction is characterized by what?

A

equilibrium constant

85
Q

it is the equilibrium constant for reactions involving enzymes

A

Keq

86
Q

reactions where rates double when substrate concentration is doubled

A

uncatalyzed chemical reactions

87
Q

reactions where the rate of the reaction initially increases rapidly as the substrate concentration is increased

A

catalyzed reactions

88
Q

it is the rate of the reaction is controlled, or limited, by the speed with which the substrate is converted into product and is released

A

rate-limiting step

89
Q

the group in amino acid R groups in the active site that are involved in catalysis

A

catalytic groups

90
Q

when the shape is complementary to the shape of the substrate

A

the substrate fits neatly into the active site of the enzyme

91
Q

mechanisms by which the enzyme attracts and holds its substrate

A

weak and noncovalent interactions

92
Q

what are some weak, noncovalent interactions

A

hydrogen bonding, van der waals forces, dipole-dipole attractions, and electrostatic attractions

93
Q

it determines the specificity of the enzyme and the only substrate that fits into the active site will be used in a reaction

A

confirmation of the active site

94
Q
  • active site is a flexible pocket that approximates the shape of the substrate
  • active site “molds” itself around the substrate
A

induced fit model

95
Q

it is the ability of an enzyme to bind only one, or a very few, substrates

A

enzyme specificity

96
Q

if the wrong amino acid is attached to the transfer RNA

A

may produce a nonfunctional protein

97
Q

what do you the similar molecules containing the same functional group

A

group specificity

98
Q

it is the formation or breakage of only certain bonds in a molecule

A

linkage specificity

99
Q

it selectively hydrolyze peptide bonds

A

proteases

100
Q

it is to distinguish one enantiomer from the other

A

stereochemical specificity

101
Q

which enzymes involved in digestion and metabolism that recognizes only those particular stereoisomers

A

D-sugars and L-amino acids

102
Q

which step is the conversion of the substrate into product

A

Step III

103
Q

which step is the release of the product and the enzyme is completely unchanged by these events

A

Step IV

104
Q

which step is which the enzyme and substrate interact, changing the substrate into a configuration that is no longer energetically stable

A

Step II

105
Q

what do you call the nonprotein group

A

cofactor

106
Q

what do you call the enzymes that require an additional nonprotein prosthetic group to function

A

cofactors and coenzymes

107
Q

what must be bound to the enzyme to maintain the correct shape of the active site

A

cofactor

108
Q

what do you call the other enzymes that require the temporary binding of a coenzyme

A

coenzyme

109
Q

at what pH number does most enzymes function best

A

pH 7

110
Q

what do you call the pH at which an enzyme functions optimally

A

pH optimum

111
Q

its when enzymes lose its biologically active configuration

A

denatured

112
Q

it is where the secretion of hydrochloric acid by cells of the stomach lining

A

stomach

113
Q

what is the pH number of a stomach

A

pH 2

114
Q

what do you call the proteolytic digestive enzyme

A

pepsin

115
Q

what do you call the proteolytic enzyme

A

trypsin

116
Q

what cleaves peptide bonds by virtually identical mechanisms

A

pepsin and trypsin

117
Q

it is a membrane bound vesicles containing about fifty different kinds of hydrolases that degrade large biological molecules into small molecules

A

lysosomes

118
Q

if the enzyme is accidentally released into the cytoplasm it may result in destruction of cellular macromolecules and death of the cell

A

lysosomal enzymes

119
Q

what pH does cytoplasmic renders them inactive

A

7.0 - 7.3

120
Q

at what celsius does our enzymes in our cells are rapidly destroyed

A

37C

121
Q

effect of temperature when more collisions occur with sufficient energy to overcome the energy barrier

A

rate of uncatalyzed reaction

122
Q

effect of temperature when it increases with modest increases in temperature

A

rate of enzyme-catalyzed reaction

123
Q

it is where the steam under pressure is pumped into the chamber until a pressure of 2 atmospheres is achieved

A

autoclaving

124
Q

how many minutes does autoclaving needs to kill the bacteria

A

20 minutes

125
Q

it is the enzymes that have more than a single bonding site

A

allosteric enzymes

126
Q

it is the small molecules that alter the active sites of allosteric enzymes by binding

A

effector molecules

127
Q

it converts the active site to an inactive configuration

A

negative allosterism

128
Q

it converts the active site to an active configuration

A

positive allosterism

129
Q

it is the first stage of the breakdown of carbohydrates to produce ATP energy

A

glycolysis

130
Q

in glycolysis what happens when the reactions of the pathway should occur more quickly

A

more energy is required

131
Q

it inhibits the activity of phosphofructokinase

A

ATP

132
Q

it regulates pathways of enzymes involved in the synthesis of a biological molecule

A

feedback inhibition

133
Q

it is the production of the enzyme in an inactive form

A

proenzymes

134
Q

chemical group is covalently added to or removed from the protein

A

protein modification

135
Q

most common type of protein modification

A

Phosphorylation or Dephosphorylation

136
Q

what adds phosphoryl groups to a target enzyme

A

protein kinases

137
Q

what removes phosphoryl groups from a target enzyme

A

phosphatases

138
Q

Enzyme inhibitors are classified on the basis of what kind when whether the inhibitor will eventually dissociate from the enzyme, releasing it in the active form

A

reversibility

139
Q

Enzyme inhibitors are classified on the basis of what kind whether the inhibitor is a structural analog, or look-alike, of the natural substrate

A

competition

140
Q

Reversible, Competitive Inhibitors are also called as

A

structural analogs

141
Q

first antimicrobics to be discovered

A

sulfa drugs

142
Q

break the peptide bonds that maintain the primary protein structure

A

proteolytic enzymes

143
Q

produced in the pancreas and transported to the small intestine

A

pancreatic serine proteases

144
Q

blood supply to the heart muscle is blocked for an extended time

A

acute myocardial infarction (AMI)

145
Q
  • first cardiac biomarker to appear
  • 30 min after onset of chest pain
  • rapidly cleared from the body by the kidneys, returning to normal levels within 16-26 h after a heart attack
A

myoglobin

146
Q
  • found primarily in muscle and the brain
  • rise 3–8 h after chest pains
A

creatine kinase - MB (CK-MB)

147
Q
  • levels return to normal after 48-72 h
  • used to diagnose a second AMI
A

creatine kinase - MB (CK-MB)

148
Q
  • only biomarker that is cardiac specific
  • any elevation is abnormal and represents cardiac injury
A

cardiac troponin I

149
Q

what is the trade of B-glucocerebrosidase

A

cerezyme

150
Q

enlargement of the spleen and liver

A

Hepatosplenomegaly

Biochemistry (5 decks)

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