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Microbiology > Chapter 8 > Flashcards

Chapter 8 Flashcards

1
Q

Metabolism

A

sum of all chemical reactions that take place in the body

  • Types of reactions: build up reactions and build down (catabolic + anabolic)
  • Goal: to stay alive
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2
Q

Metabolism: Types of Reactions

A

build up reactions and build down

  • catabolic
  • anabolic
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3
Q

Catabolic

A

Reactions that release energy by breaking complex molecules into simpler ones

  • RELEASES ENERGY
  • Synonyms: catabolism, decomposition, degradation, breakdown, hydrolysis
  • Macromolecules (nutrients)–> subunits or monomers
  • Catabolic reactions transfer energy from complex molecules to ATP
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4
Q

Anabolic

A

Reactions that require energy to synthesize complex molecules from simpler ones

  • REQUIRES ENERGY
  • Synonyms: anabolism, synthesis, condensation, build up, dehydration synthesis
  • Subunits or monomers–> macromolecules (nutrients)
  • Anabolic reactions transfer energy from ATP to complex molecules such as starch, proteins, and lipids
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5
Q

Simple Molecules

A

glucose, amino acids, glycerol, fatty acids

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6
Q

Complex molecules

A

starch, proteins, and lipids

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7
Q

Glucose + Glucose=

A

Maltose

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8
Q

Glucose+ Galactose=

A

Lactose

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9
Q

Every Bond That Forms Produces What?

A

a water molecule

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10
Q

Dehydration Synthesis vs Hydrolysis

A

Dehydration Synthesis- bonds molecules together by removing water (covalent bonds)
Hydrolysis- water is added to the molecules in order to dissolve those bonds

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11
Q

Dehydration Synthesis

A

bonds molecules together by removing water (covalent bonds)

-link monomers together into polymers by releasing water

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12
Q

Hydrolysis

A

water is added to the molecules in order to dissolve those bonds created by dehydration synthesis
-breaks polymers into monomers using a water molecule

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13
Q

Levels Of Structure

A

-Primary
-Secondary
-Tertiary
-Quaternary
>As the polypeptide forms intrachain bonds and folds, it assumes a three-dimensional (tertiary) state that displays an active site (AS)
>Because each different polypeptide folds differently, each apoenzyme will have a differently shaped active site
>More complex enzymes have a quaternary structure consisting of more than one polypeptide. The active sites (AS) may be formed by the junction of two polypeptides

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14
Q

Keratin Fiber

A

in hair and nails

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15
Q

Hemaglobin Molecule

A

consists of globular protein subunit and a heme unit (orange circle with dot in middle on globular protein subunit)

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16
Q

Denaturation

A

-protein loses its characteristic folded shape
-becomes INACTIVE
-Methods:
>pH
>Salt
>Heat:
-Protein–> 60 degrees to 65 degrees celsius
-DNA–> 80 degrees celsius
>Enzymes

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17
Q

Cofactors

A

are either organic molecules called coenzymes or inorganic elements (metal ions) that enzymes require to become functional

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18
Q

Conjugated Enzyme Structure

A
  • Metallic cofactor
  • Coenzyme
  • Apoenzymes

Apoenzyme (protein portion; inactive)–> Cofactor (nonprotein portion; activator)–> Haloenzyme(whole enzyme; active, and a substrate attaches)

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19
Q

Enzyme: Catalase

A

breaks down hydrogen peroxide

-Metallic Cofactor Required: Iron (Fe)

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20
Q

Enzyme: Oxidase

A

Adds electrons to oxygen

-Metallic Cofactor Required: Iron, copper (Cu)

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21
Q

Enzyme: Hexokinase

A

transfers phosphate to glucose

-Metallic Cofactor Required: Magnesium (Mg)

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22
Q

Enzyme: Urease

A

splits urea into an ammonium ion

-Metallic Cofactor Required: Nickel (Ni)

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23
Q

Enzyme: Nitrate reductase

A

Reduces nitrate to nitrite

-Metallic Cofactor Required: Molybdenum (Mo)

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24
Q

Enzyme: DNA polymerase

A

synthesis of DNA

-Metallic Cofactor Required: Zinc (Zn) and Mg

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25
Botulinum toxin
Hydrolyzes protein needed for vesicle transport | -Metallic Cofactor Required: Zinc (Zn)
26
Catalysis
The process by which a substance speeds up a chemical reaction but is not consumed or altered in the process
27
Enzyme Catalyzed Synthesis: Condensation Reaction
forming a glycosidic bond between 2 glucose molecules to generate maltose requires the removal of a water molecule and energy from ATP
28
Hydrolysis Reaction
breaking a peptide bond between two amino acids requires a water molecule that adds OH to one amino acid and H to the other
29
Enzyme: Oxidoreductase | Type of Chemical reaction
oxidation-reduction in which oxygen and hydrogen are gained or lost ex: Cytochrome oxidase, lactate dehydrogenase
30
Enzyme: Transferase | Type of Chemical reaction
Transfer of functional groups, such as an amino acid group, acetyl group, or phosphate group ex: Acetate kinase, alanine deaminase
31
Enzyme: Hydrolase | Type of Chemical reaction
hydrolysis (addition of water) | ex: DNAse, amylase, Lipase, sucrase, maltase, hyaluronidase
32
Enzyme: Lyase | Type of Chemical reaction
removal of groups of atoms without hydrolysis | ex: Oxalate decarboxylase, isocitrate lyase
33
Enzyme: Isomerase | Type of Chemical reaction
rearrangement of atoms within a molecule | ex: Glucose-phosphate isomerase, alanine racemase
34
Enzyme: Ligase | Type of Chemical reaction
joining of two molecules (using energy usually derived from the breakdown of ATP) ex: Acetyl-CoA synthetase, DNA ligase
35
Polymerase anabolic or catabolic?
anabolic
36
Catalase is anabolic or catabolic?
catabolic
37
Enzyme: Lactase
Systematic Name: B(beta)-D-galactosidase Enzyme Class: Hydrolase Substrate: Lactose Action: breaks lactose down into glucose and galactose
38
Enzyme: Penicillinase
Systematic Name: Beta-lactamase Enzyme Class: Hydrolase Substrate: Penicillin Action: Hydrolyzes beta- lactam ring
39
Enzyme: DNA polymerase
Systematic Name: DNA nucleotidyl-transferase Enzyme Class: Synthase Substrate: DNA nucleosides Action: Synthesizes a strand of DNA using the complementary strand as a model
40
Enzyme: Lactate dehydrogenase
Systematic Name: Lactate dehydrogenase (same as common name) Enzyme Class: Oxidoreductase Substrate: Pyruvic acid Action: Catalyzes the conversion of pyruvic acid to lactic acid
41
Enzyme: Oxidase
Systematic Name: Cytochrome oxidase Enzyme Class: Oxidoreductase Substrate: Molecular oxygen Action: Catalyzes the reduction (addition of electrons and hydrogen) to O2
42
Enzyme Specificity
the ability of a enzyme to bind with a specific substrate or catalyze a specific set of chemical reactions
43
Factors Influencing Enzyme Activity
- Temperature - pH - Concentration of Substrate - Presence of: 1. Competitive Inhibitors 2. Non-Competitve Inhibitors
44
Factors Influencing Enzyme Activity: Temperature
The enzymatic activity (rate of reaction catalyzed by enzyme) increases with increasing temperature until the enzyme, a protein, is denatured by heat and inactivated. At this point, the reaction rate falls steeply
45
Factors Influencing Enzyme Activity: pH
The enzyme that was illustrated in the picture is most active at about pH 5.0 The highest point of the line on the graph was at 5.0 pH
46
Factors Influencing Enzyme Activity: Concentration of Substrate
With increasing concentration of substrate molecules, the rate of reaction increases until the active sites (AS) on all the enzyme molecules are filled, at which point the maximum rate of reaction is reached
47
Factors Influencing Enzyme Activity: Presence of Competitive Inhibitors
1. both molecules compete for the active site (the normal substrate vs. competitive inhibitor with similar shape) 2. reaction proceeds (if normal substrate gets there first) 3. reaction is blocked because competitive inhibitor attached and is incapable of becoming a product
48
Factors Influencing Enzyme Activity: Presence of Non-Competitive Inhibitors
1. Enzyme-substrate reaction proceeds; products are released 2. A product of the enzyme reaction binds to the regulatory site and causes a change in the shape of the active site 3. Substrate cannot fit; enzyme action is blocked
49
Types of Enzymes based on location of action: Exoenzymes
made inside the cell (excreted outside the cell and then is active to break down large molecules)
50
Types of Enzymes based on location of action: Endoenzymes
active inside the cell (function within the cell)
51
Types of Enzymes based on location of action: Constituted Enzymes
made and used all the time | -an enzyme that is always produced
52
Types of Enzymes based on location of action: Regulated Enzymes
produced when needed -turned on and off of pathway (add more substrate; enzyme level increases, remove substrate; enzyme level is reduced)
53
One Type of Genetic Control of Enzyme Synthesis
1. DNA 2. RNA 3. Protein 4. Folds to form functional enzyme structure 5. Enzyme + Substrate--> products 6. Excess product binds to DNA and shuts down further enzyme production 7. DNA--> no RNA--> No protein--> No enzyme
54
Multienzyme Systems
1. Linear 2. Cyclic 3. Branched: - Divergent - Convergent
55
Feedback Inhibition
reaction product is used to regulate its own further production
56
Redox Reactions
1. Oxidation- loss of electrons 2. Reduction- gain of electrons hint: OILRIG C6H12O6 + 6 O2 ---> 6 CO2 + 6H2O
57
Adenosine Triphosphate (ATP)
``` Powers cellular work: -Chemical -Transport -Mechanical Produced by: -Oxidative Phosphorylation -Substrate level Phosphorylation ```
58
ADP
adenosine diphosphate
59
AMP
adenosine monophosphate
60
Carbohydrate Catabolism
most microorganisms oxidize carbohydrates as their primary energy source - Glycolysis - Aerobic Respiration - Anaerobic Respiration - Fermentation
61
Three pathways to breakdown glucose (cellular respiration)
1. AEROBIC RESPIRATION 2. ANAEROBIC RESPIRATION 3. FERMENTATION
62
Cellular Respiration
process organisms undergo to convert glucose to energy - involves 4 stages: 1. Glucose catabolism (usually glycolysis) 2. Transition or Bridge Reaction 3. Krebs Cycle 4. Electron Transport - may occur aerobically (most efficient) or anaerobically
63
4 Steps of Cellular Respiration
1. Glucose catabolism (usually glycolysis) 2. Transition or Bridge Reaction 3. Krebs cycle 4. Electron Transport
64
Other Pathways of Carbohydrate Catabolism
1. Pentose Phosphate Pathway | 2. Entner-Doudoroff Pathway
65
Other Pathways of Carbohydrate Catabolism: Pentose Phosphate Pathway
simultaneous with glycolysis | e.g. E. coli, Bacillus spp.
66
Other Pathways of Carbohydrate Catabolism: Entner-Doudoroff Pathway
alternate pathway for breakdown of glucose | -used by some Gram Negative bacteria (e.g. Pseudomonas)
67
Carbohydrate Catabolism: Glycolysis
usually the common first step in carbohydrate catabolism - Location: Cytoplasm - Oxygen Requirement: none - Reactant: glucose - By Products: NADH, ATP (4-2=2 net) - Final Product: 2 pyruvates (C3) (becomes the reactant of next step)
68
Metabolic Pathway
1. Glycolysis -Aerobic Respiration 2. Transition or Bridge Reaction 3. Krebs Cycle 4. Electron Transport Chain Final electron acceptor= Oxygen
69
Metabolic Pathway: Aerobic Respiration
aerobic catabolism of nutrients to carbon dioxide, water and energy, and involves an electron transport system in which molecular oxygen is the final electron acceptor C6H12O6 + 6 O2--> 6 CO2 + 6 H2O + ATP
70
Aerobic Respiration: Transition/ Bridge Reaction
``` 2nd stage -Location: >Prokaryotic Cell: cytoplasm >Eukaryotic Cell: Mitochondrial matrix -Reactant: pyruvate (C3) -Products: CO2 NADH -Final Product: Acteyl CoA (C2) (product of step 2, reactant of step 3 in pathway) ```
71
Aerobic Respiration: Krebs Cycle
``` 3rd stage -C2--> 0C -Location: >Prokaryotic Cell: Cytoplasm >Eukaryotic Cell: Mitochondrial Matrix -Reactant: acetyl CoA (C2) -Products: CO2 ATP -Final Products: NADH FADH2 (product of step 3; reactants of step 4) ```
72
Aerobic Respiration: Electron Transport
``` 4th stage -Location: >Prokaryotic Cell: plasma membrane >Eukaryotic Cell: mitochondrial inner membrane -Reactant: NADH FADH2 -Products: ATP -Final Product: H20 -Final Electron Acceptor: Oxygen ```
73
Metabolic Pathway: Anaerobic Respiration
-Location: >Prokaryotic Cell: plasma membrane >Eukaryotic Cell: mitochondrial inner membrane -Reactant: NADH FADH2 -Products: less ATP -Final Product: NO2- N2O N2 H2S CH4 -Final Electron Acceptor: Not O2 (inorganic oxygen containing molecules)
74
Metabolic Pathway: Acid + Alcohol Fermentation
- species specific - Heterolactic: yields carbon dioxide and ethanol in addition to lactic acid (organism produce lactic acid and other things) - Homolactic: one molecule of glucose is ultimately converted to 2 molecules of lactic acid (organisms produce only lactic acid)
75
Electron Transport
1. e- (enzymes) passed down electrical gradient 2. H+ "pushed" up concentration gradient from matrix to inner membrane space using energy released from e- 3. H+ "fall" back down concentration gradient providing force that joins Pi to ADP producing ATP 4. H+ and e- join up with O to form final end product WATER - final e- acceptor is Oxygen

Microbiology (20 decks)

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