Exam 2: Ch 7: Microbial Metabolism Flashcards

1
Q

Metabolism

A

pertains to all chemical reactions and physical workings of the cell

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2
Q

Anabolism

A

synthesis of molecules - building stuff up
requires input of energy
need to take smaller molecules & ATP to make larger molecules

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3
Q

Catabolism

A

breaks the bonds of larger molecules - breaking stuff down
releases energy
take larger molecules & get smaller molecules and energy

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4
Q

Electron transfer

A

allows energy to be captured in high-energy bonds in ATP and similar molecules
All catabolic reactions involve it & Cellular respiration is built on it
Directly related to oxidation & reduction electron being passed from one protein to another
By transferring the e-, energy is transferred from A → B

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5
Q

Oxidation

A

loss of electrons

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6
Q

Reduction

A

gaining of electron

the charge is reduced but it now has more energy than it did before

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7
Q

Oxidoreductase

A

enzymes that remove electrons from one substrate and add them to another
their coenzyme carriers are NAD+ and FAD
H+ is often going along in this process

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8
Q

Activation energy

A

the minimal amt of energy required to be available for bonds to be formed or broken
can be in the form of temp, pressure, etc to increase the number of particle collisions (we don’t have time to wait, so we speed up the reaction with heat/pressure/etc)

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9
Q

Why do humans need enzymes?

A

The temp and pressure that humans and bacteria would require for their chemical reactions would kill them – so we need ENZYMES
Enzymes reduce the amt of activation energy needed for chemical reactions and speed them up so that life can continue

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10
Q

Enzymes

A

reduce the amt of activation energy needed for chemical reactions
have specific active sites that bind to specific substrates
Bonds formed btwn the substrate and enzyme are weak and easily reversible
Enzymes are fast!
The # of substrate molecules converted per enzyme per second
Catalase – reacts several million times/sec
Lactase dehydrogenase – reacts a thousand times/sec

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11
Q

Specific active sites

A

arise due to the folding of a protein (folding is what allows for active sites and the activity of enzymes)
One little change could change the enzyme and make it useless

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12
Q

Substrates

A

specifically bind to active sites on the enzyme

lock & key

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13
Q

What happens at the end of enzyme-substrate reactions?

A

once the reaction is complete, the product is released and the enzyme reused

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14
Q

Cofactors

A

participate in precise functions btwn the enzyme and substrate
help bring the active site and substrate close together
participate directly in chemical reactions with the enzyme substrate complex
The need for trace elements for microorganisms arises from their roles as cofactors for enzymes

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15
Q

Coenzymes (vitamins)

A

organic compounds that work in conjunction with an enzyme
remove a chemical group from one substrate molecule and add it to another substrate molecule
Carry and transfer hydrogen atoms, electrons, carbon dioxide, and amino groups

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16
Q

Apoenzyme

A

globular protein that is the main enzyme portion

“the protein part”

17
Q

How do we regulate enzymes?

A

Adjust for the level you need at that particular time and in that particular situation
use constitutive & regulated enzymes
negative feedback loop
helps reduce waste from making enzymes that arent needed

18
Q

Constitutive enzymes

A

always present in relatively constant amounts regardless of the amount of substrate
keep substrate up → turn the enzyme down
ex. catalase

19
Q

Regulated enzymes

A

production is turned on (induced) or turned off (repressed) in responses to changes in concentration of the substrate
regulated thru gene expression

20
Q

How is enzyme function regulated?

A

Activity of enzymes influenced by the cell’s environment (natural temp, pH, osmotic pressure)

Denaturation - the weak bonds that maintain native shape of enzyme are broken

21
Q

Competitive inhibition

A

inhibits enzyme activity by supplying a molecule that resembles the enzymes normal substrate
“mimic” occupies the active site, preventing the actual substrate from binding
Actually binds to active site

22
Q

Noncompetitive inhibition

A

bind to an “allosteric” or “other” site on the enzyme, not the active site
Changes the configuration of the active site so the normal substrate cant bind

23
Q

Metabolic pathways

A

Often occur in a multistep series/ pathway
each step catalyzed by an enzyme

Metabolic pathways do not stand alone - they are interconnected and merge at many sites

24
Q

Linear pathway

A

production of one reaction is the reactant (substrate) for the next
linear chain reaction
if an enzyme gets cut out, you dont get the next step

25
Q

Branched pathway

A

Many pathways have branches that provide alternate methods for nutrient processing
fixes the problem in linear where a cut enzyme inhibits the rest

26
Q

Divergent branched pathway

A

taking 1 thing and making multiple things from it

1 input and 2 different outputs/directions

27
Q

Convergent branched pathway

A

multiple things can make 1 thing

28
Q

Cyclic pathway

A

starting molecule is regenerated to initiate another turn of the cycle
start w/a molecule and get back to that molecule

29
Q

Electron carriers

A

Cell’s reducing power
NAD+ and FAD
Carriers resemble shuttles that load and unload electrons and hydrogens to facilitate transfer of redox energy

Electrons available in NADH and FADH2

Electrons are transferred in many cases along w/protons as hydrogen atoms since one hydrogen atom (H) = 1 proton (H+) plus 1 electron (e-)

30
Q

Adenosine Triphosphate (ATP)

A

Three part molecule:
-Nitrogen base (adenine)
-5-carbon sugar (ribose)
-chain of 3 phosphate groups bonded to ribose
Can be used to phosphorylate an organic molecule (ex. phosphorylation of glucose activates its catabolism)
Phosphate groups: bulky and carry negative charges –> cause a strain btwn the last 2 phosphates making it very volatile
No storage aspects of ATP because its so unstable – its your “right now” energy

31
Q

Aerobic respiration

A

series of reactions that converts glucose to CO2 and allows the cell to recover significant amounts of energy
Complete breakdown of pyruvic acid into inorganic molecules
FEA - O2 (free O2)

Characteristic of many fungi, bacteria, protozoa, and animals

32
Q

Anaerobic respiration

A

FEA: NO3-, SO42-, CO33- and other oxidized compounds

Like aerobic respiration – there is a complete breakdown of pyruvic acid into inorganic molecules
Unlike aerobic respiration – does not use all of the steps in the Kreb’s cycle

33
Q

Fermentation

A

lots of sugar and no oxygen
Unlike aerobic and anaerobic respiration, pyruvic acid is not completely broken down into inorganic molecules
Pyruvic acid is partially broken down into organic compounds that are the final electron acceptors