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165 Cards in this Set

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Test: Which of the pathways produces 1 ATP by substrate level phosphorylation from each glucose molecule consumed?
E-D Pathway
Test: During fermentation, ATP is produced by...
Substrate level phosphorylation
Test: This enzyme acts like an extremely small electric motor...
ATPase
Test: In the real world, where available oxygen is often limiting, it is most likely that a facultative anaerobe will...
Carry on a mixture of respiration and fermentation
Test: The most commonly used amino group donor for biosynthesis is:
Glutamate
Test: Which of the following entails the largest expense in the ethanol industry?
-Capital Investment
-Feedstock cost
-Tax incentives
-Political bribes
Feedstock Cost
What is an energy carrier?
Molecules that gain and release small amounts of energy in reversable reactions.
What is the chemical composition of ATP?
The nitrogen base Adenine, a sugar Ribose, and 3 Phosphates
Under physiological conditions, ATP always complexes with what ion? What purpose does the ion serve?
Magnesium (Mg2+); it helps to neutralize the negative charge of the ATP phosphates. This stabilizes the structure in solution.
Is the phosphorylation of ADP to ATP a positive delta-G reaction or a negative delta-G reaction?
Positive; Energy is consumed to add another phosphate.
What are 3 ways that ATP transfers energy to a cell?
hydrolysis releasing phosphate; hydrolysis releasing pyrophosphate; and phosphorylation of an organic molecule.
Who is credited with the discovery of sulfa drugs?
Gerhard Domagk
How do sulfa drugs work?
Sulfanilamide is an analog of para-aminobenzoic acid (PABA), a precusor of folic acid, a vitamin necessary for nucleic acid synthesis. The drug stops bacterial growth by inhibiting the conversion of PABA to folic acid.
Who discovered streptomyocin?
Selman Waksman
Who discovered salvarsan and what is it used for?
Paul Ehrlich; it was used to treat syphilis
What is selective toxicity?
The ability of an antimicrobial agent to kill the pathogen without harming the host organism.
What is the difference between bacteriocidal antibiotics and bacteriastatic antibiotics?
Bacteriocidal drugs kill the bacteria, bacteriostatic drugs inhibit bacterial growth
What are the 6 classic targets of antibiotic drugs?
1. Cell Wall
2. Cell Membrane
3. DNA synthesis
4. RNA synthesis
5. Protein synthesis
6. Metabolism
Why is the cell wall such an obvious target for antibiotic developers?
Animal cells do contain peptidoglycan.
What enzyme is responsible for the linkage of NAG and NAM subunits during peptidoglycan synthesis?
Transglycosylase
What enzyme catalyzes the formation of peptide cross-links in peptidoglycan?
Transpeptidase
How do Beta-lactam drugs work?
They bind to transpeptidase and/ or transglycolase causing inactivation which, in turn, inhibits growth of the cell wall... leads to cell lysis
What type of bacterial cells are "cell wall" antibiotics generally used for?
growing cells
How does bacitracin work?
It binds to the bactoprenol lipid carrier molecule and prevents normal transport of monoisomeric units of peptidoglycan across the cell membrane, thus inhibiting growth of the cell wall... cell eventually lysis.
Name four types of antibiotics that target the cell wall...
1. beta-lactams

2. bacitracin

3. cycloserine

4. Vancomyocin
Name 3 types of penicillins...
1. carbenicillin

2. penicillin

3. amphicillin
Is there a beta-lactam drug that will work against beta-lactamase bacteria?
Yes, methicillin works against most beta-lactam resistant bacteria
Why isn't penicillin used when treating gram negative bacteria? What is used istead?
Penicillin has difficulty penetrating the outer membranes of gram-negative bacteria.

As such, ampicillin is generally used to treat beta-lactam susceptible gram-negative bacteria since it has a modified R-group that allows it to penetrate the outer-membrane more easily.
What cell wall targeting drug is used to treat methicillin resistant S. aureus? How does it work?
vancomyocin... it binds to the D-ala-D-ala end of the disaccharide unit and prevents action of transpeptidase and transglycolase.
What are some disadvantages of sulfa drugs?
They are bacteriostatic.

They have a narrow spectrum.

They are ineffective with high cell number.
What is an advantage of sulfa drugs?
They have selective toxicity... humans don't make folate
How were sulfa drugs invented?
Gerhard Domagk treated his daughter's strep infection with Protonsil (red dye).... the body converted the dye to sulfanilamide which is toxic to strep.
What type of drug is ciprofloxacin? What does it do?
Cipro is a fuoro-carboxy-quinoline. It is a synthetic antimicrobial.

It inhibits DNA synthesis by targeting topoisomerases such as DNA gyrase.
What are some advantages of Cipro?
1. It has selective toxicity
2. Broad spectrum
3. Bactericidal
What are some disadvantages of Cipro?
1. Resistance is rare, but high level when it occurs

2. Less effective against anaerobes
Name two classes of antibiotics that interfere with the 30S ribosomal subunit.
Aminoglycosides and Tetracyclines
Name the five classes of antibiotics that interfere with the 50S ribosomal subunit.
1. macrolides
2. lincosamides
3. chloramphenicol
4. oxazolidinones
5. streptogramins
This is the first new class of antibiotics discovered in the last 35 years.
oxazolidinones... bind to the 23S rRNA in the 50S subunit and prevent the formation of the protein synthesis 70S ribosomal complex.
To what class does streptomyocin belong and what does it do?
Aminoglycosides; Prevents 30S and 50S subunits from binding to each other
Aminoglycosides do what?
Prevents 30S and 50S subunits from binding to each other
What do tetracyclines do?
They bind to the small ribosomal subunit (30S) and block the binding of aminoacyl-tRNA.
These drugs bind to the small ribosomal subunit (30S) and block the binding of aminoacyl-tRNA.
Tetracyclines
Macrolides, chloramphenicol, and lincosamides all:
Bind to the large ribosomal subunit (50S) and block peptide transfer.
What is erythromycin?
One of many translation inhibitors

A macrolide... binds to 50S subunit
What are some advantages of erythromycin?
1. Selective toxicity
2. Often used in case of penicillin allergy
What are some disadvantages of erythromycin?
1. bacteriostatic to some bacteria

2. Often used in case of penicillin alergy

3. Narrow, spectrum, does not cover gram-negative bacteria
What are the three mechanisms of disease?
Toxigenesis, tissue damage, invade host cells
4 Antibiotic Resistance Mechanisms
1. destroying the antibiotic
2. modifying the antibiotic
3. altering the target
4. drug eflux
Infection Process:
1. Establish close proximity to mucosa
2. Avoid being swept away
3. Acquire nutrients
4. Grow quickly enough to increase and maintain population
5. Avoid host defenses
What 6 things must one always determine when discussing a pathogenic disease?
1. Causative agent
2. Pathogenesis
3. Symptoms
4. Dagnosis
5. Prevention
6. Treatment
List the pathogenic details of Diphtheria
1. Causative agent: Corynebacterium diphtheriae
2. Pathogenesis: Toxigenesic... Diphtheria toxin responsible for pathogenesis
--toxin gene carried by lysogenic phage
--AB toxin
--inhibits protein synthesis
3. Symptoms:
--bull neck, pseudomembrane, strangulation, toxic cardiopathy
4. Diagnosis: throat culture, toxin serology
5. Prevention: diphtheria toxoid immunization
6. Treatment: antitoxin, erythromycin
Mode of toxin activity: Diphtheria
1. B domain binds host cell receptor
2. AB toxin endocytosed
3. A subunit is cleaved off
4. B domain facilitates A subunit escape from vacuole
5. A subunit inactivates elongation factor 2 in the ribosome... inhibits protein synthesis
What is the difference between endotoxin and exotoxin?
Eexotoxins are secreted by the bacteria. Endotoxins are only toxic once the bacterial cell is lysed.
Define: Infectious Dose (ID50)
The number of microbes required to cause disease symptoms in half of an experimental group of hosts.
What is pathogenicity?
An organisms ability to cause disease.
What is a primary pathogen?
A disease-causing microbe that can breach the defenses of a healthy host. Same as frank pathogen.
What is virulence?
A measure of the degree or severity of disease.
Low LD 50 =
High virulence
When a mosquito transfers yellow fever from an infected human to an uninfected human it is acting as a
vector through horizontal transmission.
Transmission of a disease from the host to its offspring is called:
vertical transmission
What is a portal of entry?
A way of entry into the host organism that is best suited to the pathogens mechanisms of pathgenesis
What areas of the body are generally considered free of bacteria in healthy individuals?
Eyes, lungs,cerebrospinal fluid, and bladder
Few microorganisms can penetrate the skin due to the ________ produced by closely packed cells called ________.
thick karatin armor; keratinocytes
What does SALT stand for?
skin-associated lymphoid tissue... Langerhans cells and other specialized dendritic cells that can phagocytize microbes... located just under the skin. Defense mechanism.
What are the 5 basic steps of phagocytosis?
1. Bacteria binds to cell
2. Engulfment of bacteria into phagosome
3. lysosome fuses with phagosome
4. Destruction
5. expulsion
A regulatory site on a biological molecule distinct from the ligand/substrate binding site.
Allosteric site
Metabolic pathways that are reversible and can be used for both catabolism and anabolism.
Amphibolic
The inhibition of transcription of an operon encoding catabolic proteins in the presence of a more favorable catabolite, such as glucose.
Catabolite repression
A non-protein cellular organic molecule that can carry acetyl groups and participates in metabolism.
Coenzyme A
An oxidized molecule (e.g., NAD+) that can accept electrons.
Electron acceptor
A reduced molecule (e.g., NADH) that can donate electrons.
Electron Donor
A collection of membrane proteins that converts the energy of redox reactions into a proton potential.
Electron Transport System
A glycolytic pathway in which glucose-6-phosphate isomerizes to fructose-6-phosphate, ultimately yielding 2 pyruvate, 2 ATP, and 2 NADH.
EMP or Glycolysis
Molecules in the cell, such as ATP and NADH, that serve as energy currency. They are produced during catabolic reactions, and can be used to drive energy-requiring reactions.
Energy carrier
A measure of the heat energy in a system.
Enthalpy
A glycolytic pathway in which glucose-6-phosphate is initially oxidized to 6-phospho-gluconate, and ultimately yields 1 pyruvate, 1 ATP, 1 NADH and 1 NADPH.
ED Pathway
A measure of the disorder in a system.
Entropy
A biological catalyst; a protein or RNA that can speed up the progress of a reaction without itself being changed.
Enzyme
A fermentation reaction yielding 2 ethanol and 2 CO2 as products.
Ethanolic Fermentation
An energy carrier in the cell that can donate (FADH2) or accept (FAD+) electrons.
Flavin Adenine Dinucleotide (FADH2)
In a chemical reaction, a measure of how much energy available to do work is released or required as the reaction proceeds.
Gibbs Free Energy
An alternative to the tricarboxylic acid cycle, induced under low glucose conditions.
Glyoxalate bypass
Aromatic rings containing non-carbon atoms such as the nitrogenous bases found in nucleotides.
heteroaromatic
A fermentation reaction in which the products are lactic acid, ethanol and CO2.
heterolactic fermentation
An organism that relies on external sources of organic carbon compounds for biosynthesis.
Heterotroph
The cleaving of a bond by the addition of a water molecule.
Hydrolysis
A fermentation reaction that generates lactic acid from reduction of pyruvic acid.
lactate fermentation
A complex aromatic organic compound that forms the key structural support for trees and woody stems.
lignin
Metabolism of organic compounds to yield usable energy.
organotrophy
An electron transport chain that uses diatomic oxygen as a final electron acceptor and generates a proton gradient across a membrane for the production of ATP via ATP synthase.
Oxidative Phosphorylation
An alternate glycolytic pathway in which glucose-6-phosphate is first oxidized, then decarboxylated to ribulose-5-phosphate, ultimately generating 1 ATP and 2 NADPH.
Pentose phosphate shunt (PPS)
Describe the basics of PPS
An alternate glycolytic pathway in which glucose-6-phosphate is first oxidized, then decarboxylated to ribulose-5-phosphate, ultimately generating 1 ATP and 2 NADPH.
Phenol Red Broth Test
A clinical test for particular bacterial fermentation pathways, indicating the presence or absence of particular species, based on fermentative acids changing a pH indicator.
A clinical test for particular bacterial fermentation pathways, indicating the presence or absence of particular species, based on fermentative acids changing a pH indicator.
Phenol Red Broth Test
The enzyme-catalyzed addition of a phosphoryl group onto a molecule.
phosphorylation
A group translocation system that uses phosphoenol pyruvate to transfer phosphoryl groups onto the incoming molecule.
Phosphotransferase System (PTS)
The multi-subunit enzyme that couples the oxidative decarboxylation of pyruvate to acetyl-CoA and NADH production.
Pyruvate Dehydrogenase Complex (PDC)
Formation of ATP by the enzymatic transfer of phosphate from a substrate molecule onto ADP.
Substrate-level phosphorylation
A metabolic cycle that catabolizes the acetyl group from acetyl-CoA to 2 CO2 with the concomitant production of NADH, FADH2, and ATP.
Tricarboxylic Acid Cycle (TCA Cycle)
Which of the following is a technique for measuring ATP levels in the cell?

a. x-ray crystallography
b. polymerase chain reaction
c. NMR spectroscopy
d. DNA microchip analysis
NMR Spectroscopy
ATP is both a substrate and a allosteric inhibitor for this enzyme.
Phosphofructokinase
Kinases are enzymes that...
transfer phosphate groups
What is the function of pyruvate kinase?
It catalyzes the transfer of a phosphoryl group from PEP to ADP, generating pyruvate and ATP.
How does pyruvate kinase work?
It possesses separate binding sites for substrates and allosteric factors. PEP and ADP bind to separate, but close, catalytic sites. Fructose 1, 6-biphosphate then binds to the allosteric site which causes a conformational change in the enzyme that increases activity and allows the transfer of a P from PEP to ADP... Producing ATP and Pyruvate.
Why is the production of NADPH during the PPS and ED pathways so important?
NADPH is used for reducing power in biosynthetic pathways.
Why are the priming steps in glycolysis irreversable?
They create key intermediates:

Glucose --> Glucose 6-phosphate <--> Fructose 6-phosphate -->Fructose 1, 6-Biphosphate
During glycolysis, where does oxidation create a ~P bond?
Step 1 of the second half: Glyceraldehyde 3-phosphate loses 2e and is phosphorylated to yield 1,3 bisphosphogycerate
What is step one of glycolysis? Is this reaction reversable?
Glucose is phosphorylated by reaction with ATP to yield glucose 6-phosphate. No, this is a priming reaction that yields a key intermediate.
What is step 2 of glycolysis? Is this reaction reversable?
Glucose 6-phosphate is isomerized to fructose 6-phosphate. Yes.
What is step 3 of glycolysis? Is this reaction reversable?
Fructose 6-phosphate is phosporylated by reaction with ATP to yield fructose 1,6-biphosphate. No, this is a priming raction that yields a key intermediate.
What are steps 4-5 of glycolysis? Are these reactions reversable?
Fructose 1,6-biphosphate is cleaved into glyceraldehyde 3-phosphate and (DAHP). DHAP then isomerizes to form another molecule of glyceraldehyde 3-phosphate. Yes.
What is step 6 of glycolysis? Is this reaction reversable? How many phosphates are present after this step?
Glyceraldehyde 3-phosphate loses 2e and is phosphorylated to yield 1,3-bisphosphglycerate. Yes. 2 phosphates per molecule.
What is step 7 of glycolysis? Is this reaction reversable?
A phosphoryl group is transferred to ADP from 3-bisphosphoglycerate, generating ATP and yielding 3-phosphoglycerate. Yes.
What is step 8 (3rd of 2nd half) of glycolysis? Is this reaction reversable?
3-phosphoglycerate isomerizes to 2-phosphoglycerate. Yes.
What is step 9 (4th of 2nd half) of glycolysis? Is this reaction reversable?
2-phosphoglycerate is dehydrated to yield phosphoenolpyruvate (PEP). NO. this is a key intermediate for the formation of pyruvate and another ATP.
What is the final step of glycolysis? Is this reaction reversable? What catalyzes this reaction?
A phosphoryl group is transferred from PEP to ADP, yielding pyrivate and ATP. NO. Pyruvate Kinase catalyzes this reaction.
Which steps of glycolysis yield ATP?
Step 7 (2 of 2nd H): 1,3-bisphosphoglycerate to 3-phosphoglycerate... yields one ATP.

Final Step: Pyruvate kinase catalyzes a reaction between ADP and PEP which transfers a P from PEP to ADP yielding one ATP and 1 pyruvate.
What is the net NADH production after glycolysis?
1 NADH is produced via the first step of the second half (step 6 overall). The oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate.
What is the net yield of ATP after glycolysis?
2 ATP... 2 are used during priming steps and 2 are produced per molecule of glyceraldehyde 3-phosphate totaling 4 (2 molecules per glucose). *** 4 - 2 = 2 net
What happens to glucose 6-phosphate in the ED pathway?
glucose 6-phosphate transfers 2e to NADP (yields NADPH + H). The addition of H2O yields 6-phosphogluconate
What happens to 6-phosphogluconate in the ED pathway?
It is converted to 2-Oxo-3-deoxy-6-phosphogluconate which can, in turn, become glyceraldehyde 3-phosphate and reenter glycolysis or become pyruvate.
What is the net product yield of the ED pathway?
1 ATP, 1 NADH, and 1 NADPH
What is the net product yield for the PPS?
2 NADPH
In this fermentation pathway, the enzyme pyruvate formate lyase splits pyruvate to form acetyl-CoA plus formate.
Mixed-acid fermentation
How does glucose catabolism connect to the TCA cycle?
Through pyruvate breakdown to acetyl-CoA and CO2 via PDC
The removal of CO2 and 2e is known as...
oxidative decarboxylation
What causes the formation of holes in cheese?
propionbacterium: CO2 produced causes the holes
How many turns of the TCA cycle are required to release both carbons from Ac-CoA?
2 turns
What is Zymomonas mobilis used for?
industrial ethanol production
What is baker's yeast?
S. cerevisiae... CO2 produced causes bread to rise. Also, reduces acetylaldehyde to ethanol.
What are the basic conversions that take place during the Krebs cycle? (start with Acetyl-CoA)
1. Acetyl-CoA (2C) + Oxaloacetate (4C) -->Citrate (6C)

2. Citrate undergoes oxidative decarboxylation to form 2-oxaloglutarate (5C).

3. 2-oxaloglutarate undergoes oxidative decarboxilation to form succinyl-CoA (4C)

4. Succinyl-CoA (4C) releases CoA, providing energy to p
hosphorylate ADP to ATP... To form fumarate, 2H + 2e are transferred to FAD to form FADH.

5. Fumarate incorporates water across its double bond, forming hydroxy acid malate. The increasing stability from fumarate to malate and from malate to oxaloacetate (4C)releases enough energy to form the final NADH + H. Oxaloacetate is the intermediate of the lowest energy in the cycle and is ready to accept the next acetyl-CoA.
How many NADH + H are produced per turn of the TCA cycle?
3 per turn
How many ATP are produced per turn of the TCA cycle?
1 ATP per turn
How many FADH2 are produced per turn of the TCA cyce?
1 per turn
List the four steps of pyruvate conversion to acetyl-CoA by PDC... in detail.
1. Enzyme 1 removes CO2 from pyruvate and transfers acetyl group with 2e to thiamine pyrophosphate (TPP)

2. E2 transfers acetyl group with 2e to lipoamide

3. lipoamide transfers acetyl group onto CoA forming acetyl-CoA

4. E3 transfers 2H plus 2e from E2 lipoamide to FADH2. FADH2 transfers 2H plus 2e to NADH +H.
How many e carriers are produced during central metabolism?
12 e carriers. 24 e total being carried.

-4 e by 2NADH +2H from glycolysis.
-4 e by 2NADH+2H from pyruvate to acetyl-CoA.
--16 e by 6NADH+6H and 2FADH2.

--equates to 38 H total
In the "electron tower" the more negative the value the better the...

Likewise, the more positive the value the....
more negatve = better e donor

more positive = better e acceptor
Which is a better e donor H2O (E = +820) or FADH2 (E= -220)?
FADH2... more negative = better donor
Who discovered the mechanism behind chemiosmotic theory?
Peter Mitchell
What is chemiosmotic theory?
Essentially the theory that ETS is used to generate a proton gradient or PMF which, in turn, acts as an energy source for ATP synthase during ATP production.
How many protons does it take to produce one ATP with ATP synthase?
3 protons per ATP.
What keeps F1 of ATP synthase from rotating when F0 rotates?
The knob produced from components a and b binds F1 to the membrane and prevents rotation.
How does the F1 component of ATP synthase work to catalyze ATP production?
The gamma component runs from F0 through the center of F1 and rotates with F0. The rotation of the axle causes conformational changes in F1 that catalyze ATP forming reactions.
What components make up F1 of ATP synthase?
6 alternating alpha and beta components form a cylinder with gamma component running through.
What three complexes drive electron transport?
Complex 1: substrate oxidoreductase

Complex 2: quinone pool

Complex 3: terminal oxidase.
ETS Process:

High Oxygen Level
When O2 is high, some e are donated to NDH-2 instead of NDH-1, allowing NAD to be recycled without pumping extra protons. This is necessary to avoid generating too much neg potential and too high a pH in the cytoplasm.

NDH-2 and bo
ETS Process:

Low Oxygen Level
Cytochrome bo quinol oxidase requires a high concentration of O2 to pump protons. As such, in low O2 e are transferred instead from cytochrome bd quinol oxidase, which has a higher affiinity for O2. However, bd oxidase cannot pump protons. So at low O2, expression of NDH-2 is repressed, allowing maxiaml proton pumping by NDH-1.

NDH-1 and bd
Name 6 amino acid biosynthesis families:
1. glutamate family
2. Aspartate family
3. Serine family
4. Pyruvate family
5. Aromatic family
6. Histidine family
Name the three amino acids derived from the glutamate family.
1. glutamine
2. proline
3. arginine
Name the three amino acids derived from the pyruvate family.
1. valine
2. alanine
3. leucine
Name the 5 amino acids derived from the aspartate family.
1. asparagine
2. methionine
3. threonine --> 4. Isoleucine
5. lysine
Serine family
1. cystein
2. glycine
What is the Calvin-Benson Cycle?
the pentose phosphate cycle. More importantly, it establsihes C14 as a means to test for the presence of certain compounds.
Which metabolite is the primary N donor?
Glutamate
What are the specs for the molecular chromometer? What meets these specs?
1. must be universally conserved
2. must be functionally homologous
3. must be aligned to measure differences

-->97% 16S sequence identity
Define: Mutualism
both partners benefit from specific association
Define: synergism
Syntrophy: both partners benefit, non-specific association
Define: amensalism
one partner is harmed by non-specific association
Define: parasitism
one partner is harmed by specific association
Define: neuston
air-water interface
Marine ecosystem:
1. Euphotic Zone: phototrophy possible; sfc-200m

2. Aphotic Zone: few organisms; 200m to 4000m

3. Benthos: minerals available; 10,000m
Describe mycorrhizae
fungi are essential for plant growth.

ectomycorrhizae: colonize root sfc

endomycorrhizae: invade plant roots

soil ecosystem food web: bacteria breaking down fungi
Describe the process of opsonization.
1. Antibody binds bacterium
2. Fc binds macrophage
3. Phagocytosis
4. Destruction
What cell produce antibodies? What are their "helpers?"
B lymphocytes; T lymphocytes
What are the two general categories of non-specific immunity?
intracellular and extracellular