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Microbiology > Lecture 5 - Microbial Metabolism > Flashcards

Lecture 5 - Microbial Metabolism Flashcards

1
Q

Metabolism

A

the sum total of all energy being used and released in the body

(anabolism + catabolism = metabolism)

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2
Q

Catabolism

A

the process of breaking down larger molecules into smaller molecules

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3
Q

Anabolism

A

the process of synthesizing (building up) larger molecules

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4
Q

Hydrolysis

A

water is added as a reactant to break chemical bonds

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5
Q

Dehydration Synthesis

A

water is relased as a byproduct as bonds are formed

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6
Q

rnx

A

reaction

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7
Q

Are catabolic rxns endergonic or exergonic?

A

exergonic
(releases E)

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8
Q

Are anabolic reactions endergonic or exergonic?

A

endergonic
(uses E)

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9
Q

E

A

energy

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10
Q

Energy Coupling

A

Endergonic rxns can be used to store E within the bonds.

When those bonds are broken during a catabolic rxn, the E is released (exergonic) and can be used in other endergonic synthesis rxns.

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11
Q

ATP

A

adenosine triphosphate

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12
Q

ATP synthesis

A

ADP + P + energy –> ATP

(making ATP stores E)

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13
Q

ATP degradation

A

ATP –> ADP + P + energy

(breaking down ATP releases E)

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14
Q

ADP

A

adenosine diphosphate

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15
Q

catalysts

A

increse the rate of rxns

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16
Q

Most enzymes are _____.

A

Proteins

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17
Q

How do catalysts increase the rate of rxns?

A

Catalysts work by lowering the activation E required to initiate a rxn.

Catalysts bind to the reatants for a rxn which brings the reactants in close enough proximity with the proper orientation to react efficiently.

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18
Q

Enzymes are _______.

A

catalysts

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19
Q

-ase

A

enzyme

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20
Q

Explain How the Enzyme Lactase Works

A

Lactase binds to Lactose to break it into glucose and galactose monomers.

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21
Q

Sucrase breaks apart _____.

A

Sucrose

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22
Q

-ose

A

sugar

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23
Q

Substrate

A

the molecule that an enzyme binds to and acts on

(substrates are the reactants in the rxn)

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24
Q

decarboxylase

A

removes carbon dioxide from the substrate

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25
Q

cofactor AKA

A

coenzyme

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26
Q

Cofactors are typically _____ molecules.

A

inorganic

i.e. metal ion (iron, zinc, magnesium)

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27
Q

Coenzymes are typically _______ molecules.

A

organic

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28
Q

What is the function of a cofactor/coenzyme?

A

Cofactors and Coenzymes bind to the enzymes to make the enzyme complete and functional.

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29
Q

Fe

A

Iron

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30
Q

Mg

A

Magnesium

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31
Q

Zn

A

Zinc

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32
Q

Active Site

A

Location on the Enzyme where Substrates bind

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33
Q

dehydrogenase

A

removes hydrogen from substrate

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34
Q

decarboxylase

A

removes CO2 from substrate

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35
Q

Apoenzyme

A

the inactive, protein portion of an enzyme

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36
Q

Holoenzyme

A

an active, functional enzyme

apoenzyme + cofactor = holoenzyme

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37
Q

holo-

A

whole

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38
Q

Ca

A

Calcium

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39
Q

Cofactor Critical for Blood Clotting

A

Ca (calcium)

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40
Q

4 Factors Affecting Enzymatic Activity

A
  • pH
  • temp
  • substrate concentration
  • chemical inhibitors
    (i.e. competetive and noncompetetive inhibition)
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41
Q

What affect can pH have on enzymes?

A

If the pH is too high or too low, the enzyme can denture

42
Q

denature

A

loss of a protein’s 3D structure caused by temp or changes in pH

43
Q

Structure determines ________.

A

Function

44
Q

Function determines _______.

A

Structure

45
Q

Biochemical Pathways

A

Multistep chemical reactions that require the use of multiple enzymes.

i.e the conversion of glucose into pyruvate in glycolysis is a 10-step process that requires 10 different enzymes to catalyze each reaction.

46
Q

How do high temperatures denature a protein?

A

High temps break the hydrogen bonds that give protein a 3D structure.

47
Q

Do cold temps denature proteins?

A

No, they just decrease the enzymatic activity.

Decreased Temp = Decrased Kinetic E –> Decreased Activity

48
Q

What is kinetic energy?

A

the energy of motion

49
Q

Describe the Levels of Protein Structure

A

Primary: strand of amino acids connected

Secondary: alpha-helices and beta-sheets

Tertiary Structure: 3D Globular Structure

Quaternary Structure: multiple proteins clustered together

50
Q

What affect do colder temperatures have on enzymes?

A

Colder temperatures lower the Kinetic Energy (movement of molecules) and consequently slows down enzymatic activity.

51
Q

optimum pH

A

the pH at which an enzyme is most active

Different types of enzymes have different optimum pHs.

52
Q

Optimum pH of Pepsin (found in the stomach)

A

2

53
Q

Optimum pH of Salivary Amylase

A

7

54
Q

Optimum pH of Trypsin

A

10

55
Q

Saturation Point

A

The point at which the enzymes are working at full capacity and adding more substrate will not increase how fast the reaction takes place.

56
Q

Competetive Inhibitors

A

have a similar stuctures to the substrates and can bind to the active site of the enzyme preventing the subsrate from binding

57
Q

analog

A

molecules with similar structures

58
Q

Para Amio Benzoic Acid

A

PABA
molecule used to produce folic acid

59
Q

Sulfonamide

A

competethive Inhibitor of PABA.

When sulfonamide binds to the active site instead of PABA, no rxn takes place and therefore no folic acid is produced.

60
Q

Allosteric Inhibition

A

A non-competetive inhibitor binds to the Allosteric Site on an Enzyme causing the shape of the enzyme to change.
Because structure determines function, when the shape of the enzyme (including the active site) changes it can no longer function to bind and react substate.

61
Q

2 Types of Non-Competetive Inhibition of an Enzyme

A
  • Allosteric Inhibition
  • Removal of the Cofactor
62
Q

Glycolysis

A

the breakdown of glucose into 2 molecules of pyruvate

63
Q

Reduction Rxn

A

an electron is gained

64
Q

Oxidation Rxn

A

an electron is lost

65
Q

Reduction vs Oxidation

A

LEO the lion says GER

LEO: Loses Electrons = Oxidation
GER: Gains Electrons = Reduction

OR

OIL RIG
Oxidation is Losing e-
Reduction is Gaining e-

66
Q

NAD+ –> NADH

A

reduction

67
Q

FAD –> FADH2

A

reduction

68
Q

NADH –> NAD+

A

oxidation

69
Q

FADH2 –> FAD

A

oxidation

70
Q

Adding Hydrogens indicates Oxidation or Reduction?

A

Reduction

71
Q

Removing Hydrogens indicates Oxidation or Reduction?

A

Oxidation

72
Q

oxidative phosphorylation

A

as a molecule is oxidized one is phosphorylated

73
Q

Number of Carbons in Glucose

A

6

74
Q

Number of Carbons in Pyruvate

A

3

75
Q

What is the Net ATP synthesized in Glycolysis?

A

2

(4 ATP total is produced, but 2 ATP are used in the process. 4-2=2, so the Net ATP production is 2.)

76
Q

Glycolysis is part of both _____ and _______.

A

Cellular Respiration & Fermentation

77
Q

Where does Glycolysis take place?

A

the cytosol

78
Q

Where does the preparatory rxn converting Pyruvate into Acetyl CoA take place?

A

the cytosol

79
Q

Citric Acid Cycle AKA

A

the Krebs Cycle

80
Q

Where does the citric acid cycle occur in a eukaryotic cell?

A

the matrix of the mitochondria

81
Q

Transition Rxn AKA

A

the Preparatory Rxn

82
Q

What is the Transition Rxn?

A

Converts Pyruvate into Acetyl Coenzyme A (Acetyl CoA)

83
Q

What are the Products of the Krebs’s Cycle?

A

4 CO2
6 NADH
2 FADH2
2 ATP

84
Q

NAD+ is _______ to form NADH.

A

reduced

85
Q

FAD is _______ to form FADH2.

A

reduced

86
Q

What type of rxn is taking place in the Electron Transport Chain?

A

Oxidative Phosphorylation

87
Q

NADH is ________ to form NAD+.

A

oxidized

88
Q

FADH2 is ______ to form FAD.

A

oxidized

89
Q

Location of the Electron Transport Chain in a Prokaryote

A

plasma membrane

90
Q

Location of the Electron Transport Chain in a Eukaryote

A

inner mitochondrial membrane

91
Q

What happens to the NADH and FADH2 produced during the Citric Acid Cycle?

A

they go to the electron transport chain to fuel the proton gradient which generates more ATP

92
Q

What is the purpose of the Citric Acid Cycle?

A

Acytle CoA (2C) is combined with oxaloacetate (4C) to form Citrate (6C). Through a series of steps the carbons are broken down into CO2 and E is extracted in the form of NADH and FADH2 which can then be taken through the electron transport chain to generate more ATP.

93
Q

What is the purpose of the Electron Transport Chain?

A

The Electron Transport Chain uses E from NADH and FADH2 to reduce O2 to H2O.
The E released when O2 is reduced to H2O shuttles H+ out of the mitochondrial matrix. The proton gradient formed allows H+ to “fall” back into the matrix via the ATP Synthase embedded in the inner membrane. This falling motion allows the subunits of ATP synthase to rotate and convert ADP into ATP.

94
Q

_____ is the terminal electron acceptor in the electron transport chain.

A

O2
(oxygen)

95
Q

What is the total # of ATP produced in cellular respiration?

A

38 in prokaryotes
36 in eukaryotes

96
Q

Anaerobic Respiration

A

the terminal electron acceptor is NOT oxygen

97
Q

Terminal Electron Acceptor in Denitrifying Bacteria

A

Nitrate (NO3-)

98
Q

2 Major Types of Fermentation

A

Lactic Acid Fermentation
Alcohol Fermentation

99
Q

Name 2 Bacterias that can do Lactic Acid Fermentation

A

Lactobacillus & Streptococcus

100
Q

Name 2 Microorganisms that can do Alcohol Fermentation

A

Yeast & Clostridum

101
Q

Saccharomyces

A

Genus of Yeast

Microbiology (22 decks)

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