(LE2) Microbial Metabolism Flashcards

1
Q

What are the two source categories all organisms need for proper metabolism function?

A

Carbon source and energy source

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2
Q

What are the two processes organisms acquire carbon?

A

Autotrophy: carbon comes from CO2 in the air
Heterotrophy: Carbon comes from consuming other organic matter

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3
Q

What are the processes organisms acquire energy?

A

Chemotrophy: From chemical processes
Phototrophy: light is energy source

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4
Q

What category of metabolism do plants fall into?

A

Photoautotrophs

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5
Q

What classification of metabolism are pathogens, most bacteria, fungi, protozoans, and all animals?

A

Chemoheterotrophs

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6
Q

What phase of metabolism is shown in the image? Explain this phase. Provide an example

A

Anabolism: building polymers from monomers
- energy is needed to build chemical bonds
- e.g. protein synthesis

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7
Q

What phase of metabolism is shown in the image? Explain this phase. Provide an example

A

Catabolism: breaking down polymers into monomers
- energy is released by breaking chemical bonds
- e.g. digestion

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8
Q

What is Collision Theory?

A
  • substrates must make physical contact in order for a chemical reaction to occur
  • All molecules have kinetic energy
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9
Q

What is activation energy?

A
  • the amount of energy required to get a reaction started
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10
Q

What is reaction rate?

A

the frequency of collisions containing sufficient energy to bring about a reaction

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11
Q

How can we increase reaction rates?

A
  1. Increase kinetic energy by adding heat
  2. Lower activation energy requirements
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12
Q

What are enzymes?

A

Biological catalysts that speed up the rate of chemical reactions without being used

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13
Q

How do enzymes speed up the rate of chemical reactions?

A
  1. Decrease activation energy for reactants to reach high energy transition state
  2. Ensure reactants are in the proper orientation
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14
Q

What is turnover number?

A

number of substrates converted to products per second

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15
Q

ID and define what’s indicated in the image

A

Holoenzyme: the entire structure of the enzyme

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16
Q

ID and define what’s indicated in the image

A

Cofactor: (sometimes) inorganic component, often a metal ion (e.g. HgB and Fe)

17
Q

ID and define what’s indicated in the image

A

Apoenzyme: protein component

18
Q

ID and define what’s indicated in the image

A

Coenzyme: organic non-protein component, often derived from vitamins. Forms part of the active site

19
Q

ID and define what’s indicated in the image

A

Catalytic site

20
Q

What are the steps for the metabolism of enzyme action?

A
  1. Substrate(s) bind active site of enzyme
  2. Enzyme-substrate complex forms. Substrates are in proper orientation. “Transition state”
  3. Substrate is converted to product
  4. Products released
  5. Enzyme is unchanged during reaction. Ready to catalyze another reaction
21
Q

What factors influence enzyme activity?

A
  1. Temperature
  2. pH
  3. Substrate concentration
  4. Enzyme inhibition
  5. Feedback inhibition
  6. Enzyme activation
22
Q

Why does temperature affect enzyme activity?

A

High temp denatures (unfold) protein.
Enzymes work better at higher temp in their range. (b/c substrates move faster)

23
Q

Why does pH affect enzyme activity?

A

Low and high pH denature protein

24
Q

What is the effect on bacteria when the temperature is colder than their optimum temperature for growth? Hotter?

A

Colder - Bacteriostasis: enzymes are too slow for growth
Hotter - Bacteriocidal: kills enzyme and bacteria

25
Q

How does substrate concentration affect enzyme activity?

A

Enzyme activity can slow if there are less substrates
Enzyme has max reaction rate when saturated substrate concentration is reached

26
Q

What are the two types of enzyme inhibitors?

A

Competitive Inhibitors
Non-competitive Inhibitors

27
Q

How do competitive inhibitors influence enzyme activity?

A

They are substrate analogs, so they compete for the active site

28
Q

What happens if there are more competitive inhibitors than substrates?

A

Enzyme activity slows

29
Q

Will increasing the substrate amount increase the reaction rate against competitive inhibitors? Increasing enzyme levels?

A

Increasing [S] will work. Increasing [E] will not because substrates will still be outcompeted by greater number of inhibitors

30
Q

How do non-competitive inhibitors influence enzyme activity?

A

It binds to the allosteric site, not the active site which unfolds (changes shape) the active site

31
Q

How can you increase the reaction rate against noncompetitive inhibitors?

A

Increase [E]
Not increase [S]

32
Q

What is feedback inhibition? What is an example?

A

When the end-product of an enzymatic pathway inhibits one of the earlier reactions.
e.g., Threonine converting into Isoleucine, then Isoleucine binding to the allosteric site of the enzyme until enough isoleucine is created.

33
Q

What are two types of enzyme activation? Provide examples

A
  1. Covalent modification (covalent bond; e.g. phosphorylation/dephosphorylation)
  2. Conformational change: enzyme needs to unfold to allow substrate to fit in active site. e.g. pepsinogen interacting with HCl to become Pepsin
34
Q

What are the three types of ATP production?

A
  1. Substrate-level phosphorylation
  2. Photophosphorylation
  3. Oxidative phosphorylation
35
Q

What method of ATP production is shown? What organisms perform this method?

A

Substrate-level phosphorylation: done in glycolysis
e.g. fermenters -> slow growth. 2 ATP/glucose molecule

36
Q

What method of ATP production is shown? How does it work? What organisms perform this method? What is the energy yield?

A

Oxidative phosphorylation - electron energy captured in redox reaction to form phosphate bond.
e.g. aerobic/anaerobic respiration. Electron transport chain produces 34 ATP/glucose

37
Q

What are redox reactions?

A

Transfer of e-
Reduction: gain e- (gain energy)
Oxidation: loss of e- (lose energy)