microbial metabolism book Flashcards

1
Q

What are exergonic reactions

A

reactions that are spontaneous and release energy

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2
Q

what are endergonic reactions

A

reactions that require energy to proceed

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3
Q

what is anabolism

A

endergonic metabolic pathways involved in biosynthesis, converting simple molecular building blocks into more complex molecules

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4
Q

what fuels anabolism

A

cellular energy

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5
Q

what is catabolism

A

exergonic pathways that breakdown complex molecules into simpler ones

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6
Q

What are the two types of chemotrophs

A

organotrophs and lithotrophs

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7
Q

what are organotrophs

A

chemotrophs that get energy from organic compounds

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8
Q

examples of organotrophs

A

humans, fungi, prokaryotesw

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9
Q

what are lithotrophs

A

chemotriphs that get energy from inorganic compounds such as hydrogen sulfide and reduced iron

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10
Q

energy source, carbon source of chemoautotrophs

A

chemical
inorganic

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11
Q

examples of chemoautotrophs

A

hydrogen, sulfur, iron, nitrogen and carbon monoxide oxidizing bacteria

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12
Q

energy source and carbon source of chemoheterotrophs

A

chemical
organic coumpounds

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13
Q

examples of chemoheterotrophs

A

chemical
organic compounds

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14
Q

examples of chemoheterotrophs

A

all animals, most fungi, protozoa, and bacteria

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15
Q

energy source and carbon source of photoautotrophs

A

light
inorganic

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16
Q

energy source and carbon source of photoheterotrophs

A

light
organic comounds

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17
Q

examples of photoautotrophs

A

all plants, algae, cyanobacteria and green and purple sulfur bacteria

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18
Q

examples of photoheterotrophs

A

green and purple non sulfur bacteria, heliobacteria

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19
Q

what are oxidation reactions

A

reactions that remove electrons from donor molecules leaving them oxidized

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20
Q

what are reduction reactions

A

reactions that add electrons to acceptor molecules, leaving them reduced.

21
Q

what are electron carriers

A

molecules that bind to and shuttle high-energy electrons between compounds in pathways

22
Q

where do the principle electron carries originate from

A

B vitamins

23
Q

what is the most common mobile electron carrier used in catabolism

A

nicotinamide adenine dinucleotide (NAD/NADH)

24
Q

what is nad+

A

the is the oxidized form of the molecule

25
what is nadh
the reduced form of the molecule
26
What is NADP+
NAD+ that carries an extra phosphate group
27
what does NADP+ form when reduced
NADPH
28
what is FAD
the oxidized form of flavin adenine dinucleotide
29
what is FADH2
reduced form of flavin adenine dinucleotide
30
what do NAD/NADH, have in common with FAD/FADH2
they are used in energy extraction from sugars during catabolism in chemoheterotrophs
31
what do NADP+ and NADPH play an important role in
anabolic reactions and photosynthesis
32
What is adenosine monophosphate composed of
an adenine molecule bonded to a ribose molecule and a single phosphate group
33
what is ribose
a five carbon sugar found in RNA, while amp is a nucleotide in RNA
34
what is adenosine diphosphate
the second phosphate group added to amp
35
what is adding a phosphate group to a molecule called
phosphorylation
36
why are ADP and ATP unstable
phosphate groups are negatively charged and repel one another when they are arranged in series
37
what is a catalys
substance that helps speed up a chemical reaction that is not used or changed during chemical reactions
38
what are enzymes
catalysts for biochemical reaction inside a cell that play a role in cellular metabolism
39
how does an enzyme function
by lowering activation energy of a chemical reaction inside a cell
40
what is activation energy
energy needed to form or break chemical bonds and convert reactants to products
41
how do enzymes lower activation energy
by binding to the reactant molecules and holding them in such a way as to speed up the reaction
42
what are substrates
chemical reactants to which and enzyme binds
43
what is an active site
where the substrate binds
44
what is an apoenzyme
an enzyme lacking a necessary cofactor or coenzyme and is inactive
45
what is a holoenzyme
an enzyme that has its necessary associated cofactor or coenzyme
46
How does a noncompetitive inhibitor block a substrate
by inducing conformational change that reduces the affinity of the enzyme for its substrate
47
what are allosteric activators
they bind to locations on an enzyme away from the activation site inducing conformation change that increases the affinity of the active site.
48