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Biochemistry - Lecture > Enzymes and Vitamins > Flashcards

Enzymes and Vitamins Flashcards

1
Q

Are specialized proteins that function as biochemical catalysts

A

Enzymes

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2
Q

Are dietary organic compounds requiredbin very small quantities for normal cellular function

A

Vitamins

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3
Q

Is a compound, usually a protein, that acts as a catalyst for a biochemical reaction

A

Enzyme

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4
Q

Causes cellular reactions to occur millions of times faster than corresponding uncatalyzed reactions

A

Enzyme

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5
Q

en means

A

in

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6
Q

zyme means

A

yeast

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7
Q

Most enzymes are

A

globular proteins

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8
Q

Enzymes can be divided into two general structural classes:

A
  • simple enzymes - conjugated enzymes
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9
Q

Is an enzyme composed only of protein (amino acid chains)

A

simple enzymes

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10
Q

Is an enzyme that has a nonprotein part in addition to a protein part

A

Conjugated enzyme

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11
Q

Protein part of a conjugated enzyme

A

Apoenzyme

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12
Q

Nonprotein part of a conjugated enzyme

A

Cofactor

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13
Q

Often used to designate a biologically active combine apoenzyme-cofactor entity.

A

Holoenzyme

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14
Q

Is the biologically active conjugated enzyme produced from an apoenzyme and a cofactor

A

Holoenzyme

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15
Q

Apoenzyme + cofactor =

A

holoenzyme

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16
Q

Why do apoenzymes need cofactors?

A

Cofactors provide additional chemically reactive functional groups besides those present in the amino acid side chains of apoenzymes

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17
Q

Two broad categories of cofactors:

A
  • Simple metal ions
  • Small organic molecules
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18
Q

Metal ion cofactors include

A

Zn2+, Fe, and Cu

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19
Q

Small organic molecules are called

A

coenzymes

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20
Q

Is a small organic molecule that serves as a cofactor in a conjugated enzyme

A

Coenzymes

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21
Q

Are synthesized within the human body using building blocks obtained from other nutrients

A

Coenzymes

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22
Q

Enzymes are most commonly named by using a system that attempts to provide information about the ____________ of the enzyme.

A

function

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23
Q

are focal points for nomenclature

A

The type of reaction catalyzed and the substrate identity

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24
Q

Is the reactant in an enzyme-catalyzed reaction

A

Substrate

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25
Q

Is the stance upon which enzyme “acts.”

A

Substrate

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26
Q

Three important aspects of the enzyme-naming process are the following:

A
  1. The suffix -ase identifies a substance as an enzyme.
  2. The type of reaction catalyzed by an enzyme is often noted with as prefix.
  3. The identity of the substrate is often noted in addition to the type of reaction
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27
Q

Enzymes are grouped into six (6) major classes on the basis of the types of reactions they catalyze:

A
  • oxidoreductase - lyase
  • transferase - isomerase
  • hydrolase - ligase
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28
Q

An enzyme that catalyzes an oxidationreduction reaction

A

oxidoreductase

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29
Q

an oxidoreductase that removes hydrogen atoms from a molecule

A

Lactate dehydrogenase

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30
Q

example of oxidoreductase

A

Lactate dehydrogenase

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31
Q

An enzyme that catalyzes the transfer of a functional group from one molecule to another

A

Transferase

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32
Q

Two major subtypes of tranferase:

A
  • transaminases - kinases
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33
Q

Catalyzes the transfer of an amino group from one molecule to another.

A

transaminases

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34
Q

Play a major role in metabolic energyproduction reactions

A

Kinases

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35
Q

Catalyze the transfer of a phosphate group from adenosine triphosphate (ATP) to give adenosine diphosphate (ADP) and a phosphorylated product (a product containing an additional phosphate group)

A

Kinases

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36
Q

An enzyme that catalyzes a hydrolysis reaction in which the addition of a water molecule to a bond causes the bond to break

A

Hydrolase

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37
Q

are central to the process of digestion

A

Hydrolysis reactions

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38
Q

Effect the breaking of glycosidic bonds in oligo- and polysaccharides

A

Carbohydrase

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39
Q

Effect the breaking of peptide linkages in proteins

A

Proteases

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40
Q

Effect the breaking of ester linkages in triacylglycerols

A

Lipases

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41
Q

An enzyme that 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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42
Q

Effects the removal of the components of water from a double bond

A

Dehydrase

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43
Q

Effects the addition of the components of water to a double bond

A

Hydratase

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44
Q

An enzyme that catalyzes the bonding together of two molecules into one with the participation of ATP

A

Ligase

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45
Q

Subclasses of Oxidoreductase

A

Oxidases, Reductases, Dehydrogenases

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46
Q

oxidation of a substrate

A

Oxidases

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47
Q

reduction of a substrate

A

Reductases

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48
Q

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

A

Dehydrogenases

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49
Q

Subclasses of Transferases

A

Transaminases, Kinases

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50
Q

transfer of an amino group between substrates

A

Transaminases

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51
Q

transfer of a phosphate group between substrates

A

Kinases

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52
Q

Subclasses of Hydrolases

A

Lipases, Proteases, Nucleases, Carbohydrase, Phosphatases

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53
Q

hydrolysis of ester linkages in lipids

A

Lipases

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54
Q

hydrolysis of amide linkages in proteins

A

Proteases

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55
Q

hydrolysis of sugarphosphate ester bonds in nucleic acids

A

Nucleases

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56
Q

hydrolysis of glycosidic bonds in carbohydrates

A

Carbohydrase

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57
Q

hydrolysis of phosphate-ester bonds

A

Phosphatases

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58
Q

Subclasses of Lyases

A

Dehydratases, Decarboxylases, Deaminases, Hydratases

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59
Q

removal of H2O from a substrate

A

Dehydratases

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60
Q

removal of CO2 from a substrate

A

Decarboxylases

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61
Q

removal of NH2 from a substrate

A

Deaminases

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62
Q

addition of H2O to a substrate

A

Hydratases

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63
Q

Subclasses of Isomerases

A

Racemases, Mutases

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64
Q

conversion of D isomer to L isomer or vice versa

A

Racemases

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65
Q

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

A

Mutases

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66
Q

Subclasses of Ligases

A

Synthetases, Carboxylases

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67
Q

formation of a new bond between two substrates, with
participation of ATP

A

Synthetases

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68
Q

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

A

Carboxylases

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69
Q

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

A

Active Site

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70
Q

Is 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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71
Q

The active site in the enzyme has a fixed, rigid, geometrical conformation. Only substrates with a complementary geometry can be accommodated at such a site, much as a lock accepts only
certain keys.

A

Lock-and-Key Model

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72
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

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73
Q

Allows for small changes in the shape or geometry of the active site of an enzyme to accommodate a substrate

A

Induced-Fit Model

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74
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

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75
Q

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

A

Enzyme Specificity

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76
Q

Types of Enzyme Specificity

A

Absolute specificity, Group specificity, Linkage Specificity, Stereochemical specificity

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77
Q

The enzyme will catalyze only one reaction

A

Absolute specificity

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78
Q

Ex. of absolute specificity

A

Catalase

79
Q

catalyzes the conversion of hydrogen peroxide (H2O2) to O2 and H2O. Hydrogen peroxide is the only substrate it will accept.

A

Catalase

80
Q

The enzyme will act only on molecules that have a specific functional group

A

Group specificity

81
Q

Ex. of group specificty

A

Carboxypeptidase

82
Q

cleaves amino acids, one at a time, from the carboxyl end of a peptide chain

A

Carboxypeptidase

83
Q

The enzyme will act on a particular type of chemical bond, irrespective to the rest of the molecular structure.

A

Linkage Specificity

84
Q

Most general of the common specificities

A

Linkage Specificity

85
Q

The enzyme will act on a particular stereoisomer

A

Stereochemical specificity

86
Q

Factors that affect enzyme activity include:

A

temperature, pH, substrate concentration, and
enzyme concentration.

87
Q

As the temperature of an enzymatically catalyzed reaction _________________, so does the rate (velocity) of the reaction

A

increases

88
Q

Is the temperature at which an enzyme exhibits maximum activity

A

Optimum temperature

89
Q

Small changes in pH (less than one unit) can result in ____________________________

A

enzyme denaturation

90
Q

The pH at which an enzyme exhibits maximum activity

A

Optimum pH

91
Q

Maximum enzymic activity is possible only within a __________________________; outside this pH range, the protein is denatured
and activity drops sharply

A

narrow pH range

92
Q

Pepsin, which is active in the stomach, functions best at a pH of ____________

A

2.0

93
Q

Trypsin, which operates in the small intestine, functions best at a pH of

A

8.0

94
Q

Is the number of substrate molecules transformed per minute by one molecule of enzyme under optimum conditions of temperature, pH and saturation.

A

Turnover number

95
Q

Is a microorganism that thrives in extreme environment, environments in which humans and most other forms of life could not survive.

A

Extremophile

96
Q

Ex. of Extremophile

A

Acidophiles, alkaliphiles, halophiles, hyperthermophiles, piezophiles, xerophiles, cryophiles

97
Q

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

A

Extremozyme

98
Q

Is a substance that slows or stops the normal catalytic function of an enzyme by binding to it.

A

Enzyme Inhibitor

99
Q

Three modes by which inhibition takes place:

A
  • Reversible competitive inhibition
  • Reversible noncompetitive inhibition
  • Irreversible inhibition
100
Q

Is a molecule that sufficiently resembles an enzyme substrate in shape and charge distribution that it can compete with the substrate for occupancy of the enzyme’s active site.

A

Competitive Enzyme Inhibitor

101
Q

Binds to the active site and temporarily prevents substrates from occupying it, thus blocking the reaction.

A

Competitive Enzyme Inhibitor

102
Q

Decreases enzyme activity by binding to a site on an enzyme other than the active site

A

Noncompetitive Enzyme Inhibitor

103
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

104
Q

Inactivates enzymes by forming a strong covalent bond to an amino acid sidechain group at the enzyme’s active site.

A

Irreversible Enzyme Inhibitor

105
Q

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

A

Irreversible Enzyme Inhibitor

106
Q

Enzymes are catalysts and are _______________ in the reactions

A

not consumed

107
Q

The human body has _________of enzymes

A

1000s/thousands

108
Q

are the most effective catalysts known

A

Enzymes

109
Q

A few enzymes are now known to be

A

ribonucleic acids (RNA)

110
Q

Enzymes undergo all the reactions of proteins including __________

A

denaturation

111
Q

Enzyme activity is dramatically affected by:

A

– Alterations in pH
– Temperature
– Other protein denaturants

112
Q

are important for the chemically reactive enzymes

A

Cofactors

113
Q

Organic molecule cofactors: also called as

A

co-enzymes or cosubstrate

114
Q

Co-enzymes/co-substrates are derived from

A

dietary vitamins

115
Q

Cofactors are ________________________________________

A

small organic molecules or Inorganic ions

116
Q

Inorganic ion cofactors:

A
  • Typical metal ion cofactors
  • Nonmetallic ion cofactor
  • Inorganic ion cofactors derived from dietary minerals
117
Q

Typical metal ion cofactors -

A

Zn2+, Mg2+, Mn2+, and Fe2+

118
Q

Nonmetallic ion cofactor

A

Cl-

119
Q

Nomenclature: Most commonly named with
reference to their ______________

A

function

120
Q

Nomenclature: Most commonly named with
reference to their function:

A
  • Type of reaction catalyzed
    – Identity of the substrate
121
Q

In the fermentation process, sugar is converted to alcohol, therefore in this reaction _________ is the substrate

A

sugar

122
Q

Oxidation-reductions

A

Oxidoreductases

123
Q

Functional group transfer reactions

A

Transferases

124
Q

Reactions involving addition or removal of groups form
double bonds

A

Lyases

125
Q

Isomerization reactions

A

Isomerase

126
Q

Reactions involving bond formation coupled with ATP
hydrolysis

A

Ligases

127
Q

are always linked to one another

A

Oxidation and reduction reactions

128
Q

involves addition of a water molecule to a bond to cause bond breakage

A

hydrolysis reaction

129
Q

Place where substrate binds to enzyme

A

active site

130
Q

Formed due to folding and bending of the protein.

A

active site

131
Q

Usually a “crevice like” location in the enzyme

A

active site

132
Q

Forces That Determine Substrate Binding

A
  • H-bonding
  • Hydrophobic interactions
  • Electrostatic interactions
133
Q

An enzyme will catalyze a particular reaction for only one
substrate

A

Absolute Specificity

134
Q

This is most restrictive of all specificities (not common)

A

Absolute Specificity

135
Q

is an enzyme with absolute specificity for hydrogen peroxide (H2O2)

A

Catalase

136
Q

Catalase is an enzyme with absolute specificity for

A

hydrogen peroxide

137
Q

catalyzes reactions of L-amino acids but not of D-amino acids

A

L-Amino-acid oxidase

138
Q

Involves structurally similar compounds that have the same functional groups

A

Group Specificity

139
Q

Involves a particular type of bond irrespective of the structural features in the vicinity of the bond

A

Linkage Specificity

140
Q

A measure of the rate at which enzyme converts substrate to products in a biochemical reaction

A

Enzyme Activity

141
Q

Optimum temperature for human enzymes is

A

37ºC

142
Q

Increased temperature (high fever) leads to

A

decreased enzyme activity

143
Q

Drastic changes in pH can result in

A

denaturation of proteins

144
Q

Most enzymes have optimal activity in the pH range of

A

7.0 -7.5

145
Q

The _____________ the enzyme concentration, the greater
the reaction rate.

A

greater

146
Q

Organisms that thrive in extreme environments

A

Extremeophiles

147
Q

Ex. of Extremeophiles

A

Hydrothermophiles, Acidophiles, Alkaliphiles, Halophiles, Piezophiles, Cryophiles

148
Q

Optimal growth pH <3.0.

A

Acidophiles

149
Q

Optimal growth pH >9.0.

A

Alkaliphiles

150
Q

Live in highly saline conditions (>0.2 M NaCl)

A

Halophiles

151
Q

Grow under high hydrostatic pressure

A

Piezophiles

152
Q

Grow at temps <15oC

A

Cryophiles

153
Q

are high interest for industrial chemists

A

Extremozymes

154
Q

The development of commercially useful enzymes
involve the following steps:

A

– Isolation of extremophiles
– Isolation of extremophile DNA
– Amplification of extremophile DNA by polymerase chain reaction.
– Identification of genes responsible for extremozyme
production.
– Application of genetic engineering processes to produce extremozymes in bacteria.
– Commercial production of extremozymes.

155
Q

Production of enzymes for industrial applications.

A

Biotechnology industry

156
Q

Oil well drilling operations – degumming of guar gum.

A

Petroleum industry

157
Q

Two type of enzyme inhibitors:

A

Competitive Inhibitors and Noncompetitive Inhibitors

158
Q

Do not compete with the substrate for the same active site

A

Noncompetitive Inhibitors

159
Q

This is brought about by the presence of substances closely resembling the substrate in structure or having a similar group or radical in their molecule, so that they unite with the enzyme, thus competing with the natural or real substrate. The substrate is therefore prevented from entering the enzyme complex, rendering it inactive.

A

Competitive Inhibition

160
Q

is an antagonist to succinic acid for succinic dehydrogenase in carbohydrate metabolism

A

Malonic acid

161
Q

is an antagonist to para amino benzoic acid for the enzyme to form folic acid, a growth requirement for microorganisms

A

Sulfanilamide

162
Q

Example of Competitive Inhibition

A

Malonic acid and Sulfanilamide

163
Q

decreases enzyme activity by binding to the same active site as the substrate

A

competitive enzyme inhibitor

164
Q

Binds reversibly to an enzyme active site and the
inhibitor remains unchanged (no reaction occurs)

A

Reversible Competitive Inhibition

165
Q

are the same shape as the substrate and can bind to the active site. this prevents the substrate from binding and the reaction occuring

A

competitive inhibitor

166
Q

he sulfhydryl radical (SH) in many enzymes when oxidized to disulfide (-S-S-) by removal of hydrogen, renders the enzyme inactive. The inhibitors may be ferricyanides, Lewisite, mercuric benzoate, etc.

A

Oxidation-Reduction Effect

167
Q

Formation of substances resulting from the action of the
inhibitors on the co-factors of the enzyme

A

Non-Competitive Inhibitions

168
Q

is inhibited by carbon monoxide, cyanide and azide because the iron in the enzyme is prevented from reacting with molecular oxygen

A

Cytochrome oxidase

169
Q

bind to the enzyme away from the active site, the allosteric site. this causes the active site to change shape, and therefore the substrate can no longer bind, regardless of how much substrate is added

A

non-competitive inhibitors

170
Q

______________ have quaternary structure:
– Composed of two or more protein chains

A

allosteric enzymes

171
Q

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

A

Feedback Contro

172
Q

Regulators of a particular allosteric enzyme may be:

A

– Products of entirely different pathways of reaction
within the cell
– Compounds produced outside the cell (hormones)

173
Q

also known as pro-enzymes

A

Zymogens

174
Q

are “turned on” at the appropriate time and place

A

Zymogens

175
Q

Most digestive and blood-clotting enzymes are

A

proteolytic enzymes

176
Q

A process in which enzyme activity is altered by covalently modifying the structure of the enzyme

A

Covalent modification

177
Q

Involves adding or removing a group from an enzyme

A

Covalent modification

178
Q

Most common covalent modification

A

addition and removal of phosphate group

179
Q

A substance that kills bacteria or inhibits its growth

A

Antibiotic

180
Q

Many common prescription drugs exert their mode of
action by inhibiting enzymes
Examples:

A

– Angiotensin Converting Enzyme (ACE) inhibitors
– Sulfa drugs - Antibiotics
– Penicillins – Antibiotics

181
Q

Management of blood pressure and other heart
conditions

A

Angiotensin Converting Enzyme (ACE) inhibitors

182
Q

is an octapeptide hormone that increases blood pressure via constriction of blood vessels.

A

Angiotensin II

183
Q

block ACE reaction and thus reduce blood pressure

A

Angiotensin Converting Enzyme (ACE) inhibitors

184
Q

converts Angiotensin I to angiotensin II in the blood

A

Angiotensin Converting Enzyme (ACE)

185
Q

is an example of a ACE inhibitor

A

Lisinopril

186
Q

Derivatives of sulfanilamide

A

Sulfa Drugs

187
Q

Accidently discovered by Alexander Fleming in 1928

A

penicillin

188
Q

All have structures containing a four-membered Betalactam ring fused with a five-membered thiazolidine ring

A

penicillin

189
Q

catalyzes the formation of peptide cross links between polysaccharides strands in bacterial cell
walls

A

Transpeptidase

190
Q

The antibiotic ciprofloxacin hydrochloride

A

Cipro

191
Q

Considered the best broad-spectrum antibiotics because
it is effective against skin and bone infections as well as
against infections involving the urinary, gastrointestinal,
and respiratory systems

A

Cipro

192
Q

It is the drug of choice for treatment of traveler’ s
diarrhea

A

Cipro

193
Q
A

Biochemistry - Lecture (4 decks)

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