Exam 3 Flashcards

1
Q

What are the functions of the cell wall?

A

physical barrier, maintains shape of the bacterium, helps protect cells from osmotic lysis, helps protect from toxic materials, and contribute to pathogenicity

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2
Q

Where is the cell wall made?

A

Internally but is supposed to be on the external side

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3
Q

What is the cell wall made up out of?

A

The disaccharide subunit is made on the inside, so the NAM is linked to the UDP. Then the side chain is added and then NAG is added to the NAM. The disaccharide on the outside is added to the peptidoglycan chain.

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4
Q

How can the cell wall be broken by lysozyme?

A

The cell wall can be broken down by lysozyme which breaks the 1,4 bonds between the saccharides. Lysozyme is a nice way to control the number of bacteria that is on the human body.

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5
Q

What can the cell wall use to break it?

A

lysozyme, lysostaphin, B- lactam antibiotics

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6
Q

How can the cell wall be broken down by B-lactam antibiotic?

A

All antibiotics contain the beta lactic ring and this is the reason why the structure cannot be put into heat since the heat will cause the bonds to breaks apart. This antibiotic prevents the enzyme from putting the peptidoglycan cross linkages together by binding to the side chain.

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7
Q

How can the cell wall be broken down by lysostaphin?

A

Lysostaphin targets the peptidoglycan on other species of bacteria and will cause the cell to burst in a hypotonic state.

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8
Q

How is antibiotic resistance created? And why do the bacteria choose to keep it?

A

It is created when the beta-lactamase is cleaving the nitrogen bond so he antibiotic does not work anymore. Bacteria choose to keep it due to the constant creation of mutation (even to medicine that is not created yet) and the environment is the deciding factor on whether or not to keep the mutation.

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9
Q

How does Augmentin work?

A

Augmentin actually contains amoxicillin and clavulanic acid which contains the beta lactic structure so the beta-lactamase does not hydrolyze the amoxicillin but the calvulanic acid

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10
Q

How does Vancomycin work?

A

It works by using macromycin which is a bulky compounds that sits on the peptidoglycan which allows the beta-lactam ring to not be hydrolyzed.

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11
Q

What is peptidoglycan?

A

A rigid structure that lies just outside the cell membrane and a repeating sugar with peptide chain, the alternating sugars are NAG and NAM. Each peptidoglycan disaccharide subunit is NAM with a small peptide chain and NAG. NAG and NAM are both 6 carbon sugars. The side chain never comes off the NAG, only the NAM. The side chain needs to be linked together otherwise the cell wall will just fall off. They are cross linked directly from the 4th which is always alpine to the 3rd. Transpeptidase uses the delaine to make the cross inter bridge. Peptidoglycan take on helical shape because it is important for stability. Peptidoglycan can stretch in response to osmotic pressure and flexibility comes from peptide side chains. It is also porous so things can come into and out of the cell.

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12
Q

What are L and D forms and how are they related to the peptidoglycan?

A

D forms amino acids associated with NAM in peptidoglycan. D forms are stereoisomers of L forms normally found in biological proteins. They are both chirality and are not superimposable. The L form is counterclockwise and the D form is clockwise. L forms are the only ones coded for by amino acids. D forms need to made by racemes which takes L forms and makes them D forms. D forms are made because of denaturation by objects around the plasma membrane since it cannot detect D forms.

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13
Q

Gram positive bacteria

A

They have a thick outer layer of peptidoglycan, a very narrow periplasmic space, and teichoic acids in the peptidoglycan that do not anchor into the plasma membrane, have large pores through its matrix, no porins

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14
Q

Teichoic acids

A

only in gram positive bacteria, carry negative charge which contribute to overall charge of cell envelope, serve as a barrier of harmful substances

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15
Q

Lipoteichoic acids

A

help anchor the peptidoglycan into the plasma membrane

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16
Q

Gram negative bacteria

A

have a varying width in periplasmic space, thin layer of peptidoglycan, and an outer membrane composed of lipopolysaccharides, have porins and TonB proteins in its outer membrane to transfer molecules into periplasmic space

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17
Q

Glycoprotein

A

helps anchor the outer membrane to the peptidoglycan

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18
Q

Lipopolysaccharides

A

composed of lipids and carbohydrates, have lipid A, core polysaccharides, and O antigen

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19
Q

Lipid A

A

the most inner part that contains 3 fatty acids and a phosphate with 2 glucose derivatives

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20
Q

Core polysaccharides

A

made up of about 10 round sugars that tend to be unusual

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21
Q

O antigen

A

the largest chain and makes contact with the outside environment, could contains about 200 sugar and resist phagocytosis

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22
Q

Importance of LPS

A

the contribution to negative charge on cell surface, help stabilize outer membrane structure (adding rigidness), may contribute to attachment to surfaces and biofilm, creates a permeability barrier, protection from his defenses (resists entering of bio salts), and can act as a endotoxin (made inside of the cell and when released it is needed, can create shock and fever from lipid A)

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23
Q

Porin proteins

A

The outer membrane is more permeable than plasma membrane due to porins. They are usually primary proteins together and are nonspecific but molecules that are smaller than 600. They use facultative diffusion

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24
Q

How does the cell wall explain how the gram stain works?

A

Large pores in the gram-positive cell shrink while the outer membrane lipids are stripped in the gram-negative cells

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25
Flagella
used for motility, they are usually spiral, hollow, rigid filaments extending from the cell surface
26
Monotrichous
one flagellum
27
Amphitrichous
one flagellum at each end of the cell
28
Polar flagellum
flagellum at the end of the cell
29
Lophotrichous
cluster of flagella at one or both ends
30
Peritrichous
spread over entire surface of cell
31
What are the three part of the flagella?
filament, hook protein, and basal body
32
Filament
a single protein subunit made up of flagellum
33
Hook protein
connects the filament to the basal body
34
Basal body
embedded in the cell wall and is most complex, 4 rings in the gram negative while 2 rings in the gram positive, gram negative have a p ring in the peptidoglycan and c rings in the cytoplasmic part of the membrane
35
Why is the flagellum hollow in bacteria?
They are hollow because the filament extends by the tip so the proteins that the filament is made up out of will go through the center
36
How does the flagellum rotate?
like a propeller and is very rapid rotation up to 1100 rev/sec
37
What does counterclockwise rotation mean in bacteria?
run, move forward
38
What does clockwise rotation mean in bacteria?
tumble, cell stops
39
Chemotaxis
the movement toward a chemical attractant or away from a chemical repellent and changing the concentration of chemical attractants and chemical repellents bind chemoreceptors of the chemo sensing system
40
What happens in the presence of attractant?
tumbling frequency is reduced and runs in the direction of attractant are longer
41
What happens in the presence of repellent?
tumbling frequency is reduced and runs in the direction opposite from repellent are longer
42
How does the flagellum operate?
2 part motor producing torque which is rotor and stator
43
Stator
is an electromagnet so Mot A and Mot B proteins are used to help the energy needed from existing ion gradients used to turn the flagella, the flagellum moves by protons which move through the cell and allow the basal body to turn and that causes the actual turning of the filament
44
Rotor
C ring and MS ring turns and interacts with the stator
45
How do bacteria move without flagella?
gliding (smooth sliding over a surface), polymerization of action (for propulsion of bacteria into adjacent cells) and twitching (slow, jerky process using pili)
46
Pili
a secondary function that some bacteria have evolved to have, adherence molecules stick to surfaces that are mediated by pili, fibers of pili proteins possess other proteins on their tips for sticking, some scientists prefer to use pili only for conjugation structure and fimbrriae for adherence
47
Glycocalyx
outermost layer in the cell envelope, sugar coat, aids in the attachment to solid surfaces, biofilms are considered this, refers to either slime layers or capsules
48
Capsules
composed of polysaccharides, sticky, helps bacteria adhere to different things, and an organized layer helps define the structure of the cell, not easily removed from the cell, can be seen from underneath light microscopes, make it hard for the immune response to recognize you, cannot be phagocytosed from the immune system, allows you to pathogenic, lot of water to prevent desiccation
49
Slime layers
similar to capsules, sticky, can adhere to things, and much more easily removed to the cell, outermost layer, cannot be seen underneath microscope, offer protection from host cell immune response, difference antibiotics get hung up here as well, aids in motility and can cause gilding cause of slime, a lot of water to prevent desiccation
50
S layers
made up of proteins, extremely organized, help adhere to things, and can be found in both positive (adheres to our layer) and negative (adheres to peptidoglycan) bacteria, gives protection, helps with shapes and rigidity, has potential in nanotechnology, protects from ions and pH fluctuation and osmotic stress, enzymes and predation, is self assembly so no energy or enzyme needed
51
Sporulation
complex 7 step process, has to put all layers together, all of nothing response, cannot stop in the middle, and usually occurs up to 10 hours, triggered my nutrient starvation, the master regulator is spo A and once it has phosphorylated it has started
52
Steps in sporulation
axial filament forming so the chromosome is stretching out the entire length of organism, then septum formation which is a forespore development (separation between forespores and the rest of cell) then engulfment of forespore, then cortex formation which is specialized peptidoglycan formation for the cortex, then coat synthesis, then completion of coat synthesis and should be resistant to everything it is supposed to have then release to the environment which kills mother cells
53
Germination
reverse of sporulation and it still a complex multistep process, transformation of sporulation into a vegetative cell
54
Steps of germination
activation - heat for 70 degrees Celsius for 10 minutes, germination - germinate receptor binds certain nutrients when they bind so it trigger a lot of things to happen in the cell, water starts to move back into the cell so calcium increase which starts metabolic activity, the cell will swell and the cortex region degrades, outgrow - emergence of vegetative cell
55
What is the size and shape of Archaea?
usually between 0.5 and 5 micrometers in diameter but can vary greatly, they have similar shapes, are singular, circular chromosomes, and lack a membrane-bound nucleus, shapes can also vary so they can be rods, spheres or spirals just like bacteria
56
Cytoplasm in archaea
Histones form structures that DNA wraps around. Histones are difference in archaea from eukarya. There is a single circular chromosome. The thought is bacteria had branched off from eukarya and archaea then separated from each other. The histone is smaller in archaea since there is only a tetramer so the DNA has to wrap around a smaller space
57
Cytoskeleton in archaea
The cytoskeleton shows that archaea can resemble eukarya but some resemble bacteria. They are playin the same role as bacteria when they are closer in relation to bacteria
58
Plasma membrane in archaea
all archaeans possess a plasma membrane because it is needed, can be bilayer or monolayer, contains hydrocarbons derived from isoprene units, hydrocarbons attached to glycerol by ether linkages, have a transport system, lipid chain has an isoprene unit which is 5 carbon units, fatty acids is attached to the glycerol with ester linkages, fatty acids attach to the 1 carbon in archaea while 3 carbon in bacteria, does play the same role in archaea, not able to use group translocation, so have primary and secondary active transport
59
Cell wall in archaea
most have a cell wall but is not needed, provides physical and osmotic protection, function is the same, look the same as bacteria, uses NAG and NAT which have the peptide side and there is no D forms, only L forms, joined by beta 1,3 linkage, lysozyme and beta lactase antibiotic will not work on archaea
60
Flagella in archaea
Flagellum is similar to bacteria that they rotate to move the cell. They are not evolutionary related to bacteria but more to pili, thinner, usually composed of 2 or more different version of flagellin protein, and likely growing from base rather than tip, not hollow, basal body is much less complex, tend of rotate slower and needs ATP to move the basal body, very stable because it has to withstand various conditions, no tumble, rotation one way gives forward while rotating in the other gives backward
61
S layer in archaea
a single layer of many identical armor like subunits, made up of polysaccharides and use it the same way that bacteria does, sticky so helps with adherence
62
Cannulae in archaea
hollow glycoprotein tube that links cell together to form a complex network, running between archaea and what they are doing is still being researched but it could have something to do with sharing connections or sharing nutrients
63
Metabolism
sum of the chemical reactions in an organism
64
Catabolism
the breakdown of molecules for energy, reducing potential, and building blocks, an energy conserving reaction, fueling reaction, providing a ready source for reducing power, generating precursors for biosynthesis, and they break down macromolecules and store the energy for later as ATP
65
Anabolism
put energy together so it is the energy using process, the synthesis of complex organic molecules from simpler ones, requires energy from fueling reactions, and takes simple sugars and puts them together to make macromolecules
66
How is metabolism, catabolism and anabolism related?
Catabolism proves the building blocks and energy for anabolism and then catabolic reactions transfer energy from complex molecules to ATP, anabolic reactions transfer energy from ATP to complex molecules
67
Metabolic pathways
are long, complex, branched and mediated by enzymes that are encoded by genes
68
Enzymes
acts as catalysts, they are either used up or charged, the active of an enzyme is vital to its function, if it were to lose the structure of the active site, it will lose it function, all enzymes have a turnover number as well, meaning how fast it works, this number is usually between 1-10,000 molecules per second, are not spontaneous because of their high affinity, solely composed of one or more polypeptides, and others are composed of peptides and non protein components
69
Transition state
higher when an enzyme is not added
70
Activation energy
energy requires to bring reacting molecules together in a specific way, the greater the activation energy the slower it occurs, enzymes lower activation energy because of their high affinity, meaning they can pull things towards them, also physically grateful what they need to binds and make it react with each other
71
Lock and key model
enzyme is the lock and substrate is the key and the active state is the key hole, really rigid
72
Induced fit
differs from lock and key, substrate plays a role in shape of the enzyme and the enzyme will hug you a bit, the substrate still has to have a very specific confirmation with the enzyme, when the substrate binds it affects ends conformation of the enzyme so enzyme changes just as much as substrate
73
Apoenzyme
protein component of an enzyme, it is inactive if alone and needs a cofactor to be become active
74
Holoenzyme
active form of an enzyme which is the apoenzyme and cofactor together
75
Co-factor
non protein component that some enzymes need to work
76
Coenzymes
loosely attached to protein portions of the enzyme and organic molecules, they are carrier by moving functional groups substrate to substrate important coenzymes
77
Prosthetic
closely attached and tend to be inorganic
78
Substrate important enzymes
NAD+, NADP+, FAD, Coenzyme A, and most of them are involved in the TCA cycle
79
What are the environmental factors on enzymes?
temperature and pH and the active site becomes denatured
80
How does temperature affect enzymes?
every enzyme has a temperature has an optimal temperature, at high temperatures, the enzyme starts to pull apart, they denature, and the active site disappears, at low temperatures, the enzyme starts to not work fast enough and eventually shuts down
81
How does pH affect enzymes?
has an optimal pH range, they cannot function if it gets too acidic or alkaline, it dentures when it passes the range
82
How does substrate concentration affect enzymes?
It effects product formation and then when you increase, more products will be made
83
Km
when enzymes have to work at half of its capacity, used to measure affinity an enzyme has for its substrate, low Km is good at grabbing substrate in the environment, high Km needs more substrate in the environment and not the best at grabbing it, most enzymes tend to have low Km
84
Vmax
the rate of product formation when the enzymes is saturated with substrate and operating as fast as possible
85
Michaelis Menten Plot
up to a point of adding too much substrate and all enzymes are busy with substrate then it does not matter if you add more substrate because enzymes are saturated with substrates
86
Competitive inhibition
when the competitor directly competes with the binding of substrate to active site so substrate cannot bind to active site since inhibitor is there
87
Example of competitive inhibition
PABA sulfonamides that work at folic acid pathways
88
The ways of overcoming competitive inhibitors
having a higher substrate concentration, enzymes have higher affinity for competitive inhibitors
89
Noncompetitive inhibition
when a competitor binds to enzymes at allosteric sites, this changes the enzymes shape so that it becomes less active, does not bind to the active site
90
The ways of overcoming noncompetitive inhibitors
using heavy metals like mercury or use side groups
91
Metabolic regulation
the conservation of energy and materials and the maintenance of metabolic balance despite changes in environment
92
3 major mechanisms of metabolic regulation
metabolic channeling, direct stimulation, regulation of the synthesis of a particular enzyme
93
Metabolic channeling
moving enzymes around to appropriate places within the cell depending on cell needs,
94
Regulation of the synthesis of a particular enzyme
gene expression, whether this needs to be made or not
95
Direct simulation
gene expression - turned on or off
96
Allosteric regulation
most regulatory enzyme, binds non covalently to the regulatory site and changes the shape of the enzyme and laters the activity of the catalytic site, very specific and tightly controlled process
97
Positive allosteric regulation
turns on so increases enzyme activity
98
Negative allosteric regulation
turns off so inhibits enzyme activity
99
Covalent modification
a reversible on and off switch which works by adding or removing functional groups to enzymes and turning it off or on by doing this and then the addition or removal of a chemical group, can respond to more stimuli in varied ways, regulation of enzymes that catalyze covalent modification adds a second level, there is a finer level of control compared to allosteric
100
Feedback inhibition
the products can be used to turn it off, the ends product will bind to the metabolic pathway and turn off the feedback