nitrogen metabolism Flashcards

1
Q

Conversion of ammonia to nitrates

A

Nitrification (via reduction)
- ammonia is oxidized

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2
Q

Process by which nitrates and nitrites are broken down to molecular nitrogen

A

Denitrification
- broken down to release nitrogen gas back into the atmosphere

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3
Q

the process of turning nitrogen gas from the air (N₂) into ammonia (NH₃) or ammonium ions (NH₄⁺) that plants can use

A

Nitrogen Fixation
- Reduction of N2 to NH3
- Plants and animals cannot carry out nitrogen fixation

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4
Q

As plants and animals can’t do this on their own. How does special bacteria handle this process.

A

These bacteria often live in partnership with plants, forming small bumps (called nodules) on the roots of plants like beans, peas, and other legumes.

The bacteria use nitrogenase to convert nitrogen gas into a usable form. It adds six electrons to nitrogen gas = ammonium ions.
Ammonium ions are an essential form of nitrogen that plants can absorb and use to grow.

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5
Q

Why is ammonia important in nitrogen fixation

A

Ammonia (NH₃) is one of the main ways nitrogen becomes available for living things.
It’s the only natural source of nitrogen in the biosphere, apart from nitrates (another usable form of nitrogen).

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6
Q

How do living things use ammonia?

A

Ammonia can turn into ammonium ions (NH₄⁺), which plants use as a building block to make important compounds like proteins and DNA.

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7
Q

Ammonia in fertilizer

A

Scientists can make ammonia in factories by combining nitrogen (from the air) and hydrogen.
This ammonia is used to create synthetic fertilizers, which often include nitrates to help plants grow better.

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8
Q

how does the enzyme nitrogenase helps convert nitrogen gas (N₂) from the air into ammonia (NH₃)

A
  1. Binding Nitrogen Gas:
    The enzyme nitrogenase attaches to a nitrogen gas molecule (N≡N) from the air.
  2. Step-by-Step Reduction:
    The nitrogen gas molecule is reduced (changed) by adding hydrogen atoms in three stages.
    This happens with the help of a helper molecule (called a reducing agent, like ferredoxin), which supplies the hydrogen atoms.
    Each step adds 2 hydrogen atoms until the nitrogen is fully converted.
  3. Final Product:
    Once fully reduced, the nitrogen molecule turns into ammonia (NH₃).

Two molecules of ammonia are released, and the enzyme is freed to start the process again with a new nitrogen gas molecule.

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9
Q

how nitrogenase works to convert nitrogen gas (N₂) into ammonia (NH₃) with the help of several protein

A

Ferredoxin: Supplies electrons to the system.

Dinitrogenase reductase:
- iron–sulfur (Fe–S) protein
- Transfers electrons from ferredoxin to dinitrogenase. This step requires energy from ATP.

Dinitrogenase:
- iron–molybdenum (Fe–Mo) protein
- Uses the electrons to reduce nitrogen gas (N₂) into ammonia (NH₃).

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10
Q

Nitrogenase Reaction

A

The half-reaction of reduction:
6 electrons are needed to turn nitrogen gas (N₂) into ammonia (NH₃).
2 electrons are used to turn hydrogen ions (H⁺) into hydrogen gas (H₂).

The half-reaction of oxidation:
The source of electrons (needed for these reductions) depends on the organism. Different organisms use different substances to supply the electrons.

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11
Q

Process by which the final product of a series of reactions inhibits the first reaction in the series

A

Feedback Inhibition in Nitrogen Metabolism

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12
Q

in Feedback Inhibition in Nitrogen Metabolism, what happens if there is a high level of amino acids or nucleotides

A

the cell saves energy by not making these compounds through a feedback inhibition mechanism

  • Helps save energy as biosynthetic pathways for many nitrogen containing compounds are long and complex

[It’s a way for cells to turn off a process when they already have enough of a product, like amino acids or nucleotides.
If there’s a lot of these compounds, the final product signals the first step of the reaction chain to stop making more.
This saves the cell energy because making nitrogen-containing compounds involves long and complicated processes.]

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13
Q

Transfer of amino groups from one molecule to another

A

Transamination
- it is when an amino group (a part of an amino acid) is moved from one molecule to another to help make different amino acids.

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14
Q

what does amidation of glutamate gives

A

glutamine
- glutamine is made by adding another group to glutamate, a process called amidation.

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15
Q

Glutamate is formed by reductive amination of

A

a-ketoglutarate and NH4
- Glutamate is made by adding an amino group (NH₄⁺) to a molecule called α-ketoglutarate. This is called reductive amination.

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16
Q

what are the different families of amino acids based on biosynthetic pathways

A

index card

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17
Q

How is glutamate formed?

A

Glutamate is formed by combining α-ketoglutarate and ammonium (NH₄⁺) in a reaction catalyzed by glutamate dehydrogenase (GDH) using NADPH.

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18
Q

What role does glutamate play in amino acid biosynthesis?

A

Glutamate is a major donor of amino groups in many reactions, while α-ketoglutarate acts as the acceptor.

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19
Q

How is glutamine made from glutamate?

A

Glutamate undergoes amidation to form glutamine, a reaction catalyzed by glutamate synthase (GS) and requiring ATP.

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20
Q

When do GDH and GS reactions occur together?

A

When nitrogen is abundant, both GDH and GS reactions occur.

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21
Q

What happens when nitrogen is limited?

A

Only the GS reaction occurs to conserve nitrogen.

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22
Q

How is glutamate replenished?

A

By the reductive amination of α-ketoglutarate, catalyzed by the enzyme glutamate:oxoglutarate aminotransferase (GOGAT).

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23
Q

Relationship between Amino Acid Metabolism and the Citric Acid Cycle

A

ppt

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24
Q

it is the biologically active form of vitamin B6 and plays a critical role in reactions involving amino acids.

A

Pyridoxal Phosphate (PyrP)
- transamination: transfer the amino group from one molecule to another
- decarboxylation: removing a carbon dioxide group

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25
Q

What type of bond does PyrP form with an amino acid during transamination?

A

An imine (Schiff base).

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26
Q

What are the products of the transamination reaction involving PyrP?

A

An α-keto acid and pyridoxamine phosphate.

  • all transamination reactions with PyrP are reversible
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27
Q

What is the precursor molecule for serine?

A

3-phosphoglycerate.

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28
Q

Which molecule donates nitrogen to 3-phosphoglycerate in the biosynthesis of serine?

A

Glutamate

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29
Q

What is the intermediate formed during serine biosynthesis?

A

3-phosphoserine
- this is formed by removing the phosphate grp thru hydrolysis

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30
Q

What enzyme catalyzes the conversion of serine to glycine?

A

Serine hydroxymethylase.

31
Q

What is the one-carbon acceptor in the serine-to-glycine conversion?

A

Tetrahydrofolate (THF).
- derived from folic acid
- acts as a carrier fr 1-C unit
*as conversion of serine to glycine removes 1 carbon

32
Q

What is tetrahydrofolate What is the sulfur donor in the conversion of serine to cysteine in plants and bacteria?

A

3’-phospho-5’-adenylyl sulfate.

33
Q

Why do animals use methionine instead of sulfate to produce cysteine?

A

Animals lack the enzymes required for the sulfate-to-sulfide conversion.

34
Q

What is the role of serine acyltransferase in plants and bacteria?

A

It converts serine to O-acetylserine using acetyl-CoA as a donor.

35
Q

Why is methionine considered an essential amino acid?

A

Because animals cannot synthesize it and must obtain it from their diet.

36
Q

What reactive molecule is formed when methionine reacts with ATP

A

S-adenosylmethionine (SAM)
- highly reactive methyl grp
- transferred to other molecules

37
Q

What molecule carries a methyl group and produces homocysteine after hydrolysis?

A

S-adenosylmethionine (SAM).

38
Q

How is cysteine produced in animals?

A

By combining serine and homocysteine.
- the only pathway animals have for cysteine production.

39
Q

essential amino acids

A

Amino acids that the body cannot synthesize and must be obtained from the diet.
Protein deficiency: Kwashiorkor

*: Protein synthesis requires all amino acids, including those the body cannot produce

40
Q

three carriers of one-carbon units

A

Biotin - Carries CO2.
Tetrahydrofolate (THF) - Carries methylene and formyl groups.
S-adenosylmethionine (SAM) - Carries methyl groups

41
Q

amino acid catabolism

A
  1. transamination, transferring it to α-ketoglutarate = Glutamate and an α-ketoacid
    - removal of amino grp
  2. breaking down amino acid carbon skeletons
    - Glucogenic: Converts to pyruvate or oxaloacetate for glucose production.
    - Ketogenic: Converts to acetyl-CoA or acetoacetyl-CoA for ketone body production.
42
Q

What happens to the nitrogen removed from amino acids?

A

It can be reused for biosynthesis or excreted as ammonia, urea, or uric acid

43
Q

What are the end products of glucogenic and ketogenic amino acid breakdown?

A

Glucogenic: Pyruvate or oxaloacetate.
Ketogenic: Acetyl-CoA or acetoacetyl-CoA.

44
Q

What is the role of α-ketoglutarate in amino acid catabolism?

A

It accepts the amino group during transamination, forming glutamate.

45
Q

Pathway that leads to excretion of waste products of nitrogen metabolism, especially those of amino acids

A

urea cycle
- central pathway in nitrogen metabolism
- nitrogens that enter the cycle come from several sources
- linked to TCA
- involve in both anabolism and catabolism

46
Q

Where does the first step of the urea cycle occur?

A

In the mitochondria, where carbamoyl phosphate transfers its carbamoyl group to ornithine to form citrulline.

47
Q

What is the first source of nitrogen for urea?

A

Carbamoyl phosphate.

48
Q

What happens to citrulline after it is formed in the mitochondria?

A

Citrulline is transported to the cytosol via a transporter.

49
Q

What is the second source of nitrogen for urea?

A

Aspartate, which combines with citrulline to form argininosuccinate.

50
Q

What links the urea cycle to the citric acid cycle?

A

The production of fumarate during the breakdown of argininosuccinate.

51
Q

What are the final products of arginine hydrolysis in the urea cycle?

A

Urea (excreted) and ornithine (recycled back to the mitochondria).

52
Q

What is the main purpose of the urea cycle?

A

To remove excess nitrogen by converting it into urea, which is excreted in the urine.

53
Q
A
54
Q

How is fumarate produced in the urea cycle?

A

Fumarate is produced when argininosuccinate is split into fumarate and arginine by the enzyme argininosuccinate lyase.

55
Q

What happens to fumarate after its production in the urea cycle?

A

Fumarate enters the citric acid cycle, where it is converted to malate and contributes to energy metabolism.

56
Q

What is the precursor for both AMP and GMP?

A

Inosine monophosphate (IMP).

57
Q

What energy source is used for
the synthesis of AMP from IMP?
the synthesis of GMP from IMP?

A

GTP
ATP

58
Q

What enzyme catalyzes the conversion of IMP to adenylosuccinate?

A

Adenylosuccinate synthetase.

59
Q

What enzyme catalyzes the conversion of IMP to XMP?

A

IMP dehydrogenase.

60
Q

How many ATP equivalents are needed to produce GMP from ribose-5-phosphate?

A

9 ATP equivalents.

61
Q

What are the two purine bases derived during catabolism?

A

Guanine and adenine.

62
Q

What is guanine deaminated to during purine catabolism?
What is adenine deaminated to during purine catabolism?

A

Xanthine
Hypoxanthine
respectively

63
Q

What is the final product of purine degradation in humans?

A

uric acid

64
Q

What condition results from the accumulation of uric acid in joints?

A

Gout

65
Q

What drug inhibits the conversion of hypoxanthine and xanthine to uric acid?

A

Allopurinol.

66
Q

What is the purpose of salvage reactions in purine metabolism?

A

To recycle purine bases and conserve energy.

67
Q

Which enzyme recycles guanine and hypoxanthine?
Which enzyme recycles adenine?

A

Hypoxanthine-guanine phosphoribosyltransferase (HGPRT).
Adenine phosphoribosyltransferase (APRT).
respectively

68
Q

What are the two enzymes inhibited by CTP in pyrimidine nucleotide biosynthesis?

A

Aspartate transcarbamoylase and CTP synthetase.

69
Q

What does UMP inhibit in pyrimidine nucleotide biosynthesis?

A

Carbamoyl phosphate synthetase.

70
Q

What are the final products of pyrimidine catabolism?

A

Beta-alanine (from cytosine/uracil) and beta-aminoisobutyrate (from thymine).

71
Q

What enzyme reduces ribonucleoside diphosphates to deoxyribonucleoside diphosphates?

A

Ribonucleotide reductase.

72
Q

What molecule donates the methyl group to convert dUMP to dTMP?

A

Tetrahydrofolate (THF).

73
Q

Which enzyme is targeted by cancer drugs like methotrexate?

A

Dihydrofolate reductase.