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Science for Medicine > Nitrogen 1-3 > Flashcards

Nitrogen 1-3 Flashcards

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1
Q

How does Nitrogen enter the body ?

A

Through diet

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2
Q

How many covelant bonds does Nitrogen have ?

A

Three

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3
Q

What is the name of the enzyme that bacteria use to break the bonds found in Nitrogen & what affects this enzyme ?

A

Nitrogenase

Inactivated by Oxygen: Live anaerobically

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4
Q

What kind of bacteria can form structures that resemble cell walls ?

A

Cynobacteria

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5
Q

What do leguminous plants contain that assist in Oxygen binding ?

A

They produce hemoglobin

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6
Q

What form must Nitrogen be before it is taken up by bacteria & plants ?

A

Nitrate (NO3)

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7
Q

What is the product of Alpha-Ketogluterate + Ammonium ?

A

Glutamate

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8
Q

Alpha-Ketogluterate is an intermediate from which other biochemical cycle ?

A

CAC

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9
Q

What Amino Acid is crucial for Nitrogen to enter the cells of the body ?

A

Glutamate

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10
Q

What 2 Amino Acids also act as excitatory neurotransmitters ?

A

Glutamate and Aspertate

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11
Q

Define transamination?

A

An amino acid giving up an amino acid group to form a Keto-acid and an amino acid

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12
Q

Why is transamination used ?

A

To conserve Nitrogen in an organism

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13
Q

What co-factor do Amino Transferases rely on & where does this originate from ?

A

Pyridoxal Phosphate Co-factor and it is derived from Vitamin B6

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14
Q

What does L-Glutamine do ?

A

Acts as a temporary storage for Nitrogen in the body

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15
Q

Amino acids undergo oxidative catabolism under what three conditions ?

A

1: Leftover A.A. from normal turnover and degradation
2: When there is an excessive amount of dietary A.A that exceed the body’s protein synthesis.
3: During starvation protein is broken down due to the lack of carbohydrates

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16
Q

What cuts protein into peptides in the stomach ?

A

Pepsin

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17
Q

What acts in the small intestine to cut down proteins & larger peptides into smaller peptides ?

A

Trypsin and Chymotrypsin

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18
Q

What acts in the small intestine to degrade peptides into amino acids ?

A

Aminopeptidase and Carboxypeptidases A and B

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19
Q

How are active proteases stored in the small intestinal cells ?

A

Zymogens

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20
Q

What happens to defective proteins ?

A

They are regulated and broken down by proteosome into peptide fragments and Released Ubiquitin

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21
Q

How is Nitrogen excreted from the body ?

A

As urea

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22
Q

Properties of urea

A

Highly soluble and non-toxic

23
Q

What are the properties of ammonia that have to be considered when transporting through the body ?

A

Highly toxic

24
Q

how is Ammonia transported through the bloodstream ?

A

As Alanine

25
Q

What is the name of the cycle that carries Alanine from muscle to the liver via the bloodstream ?

A

Glucose-Alanine Cycle

26
Q

When would the body utilize the Glucose-Alanine Cycle ?

A

During starvation

27
Q

What other cycle is much like the Glucose-Alanine cycle and when would it be utilized ?

A

The cori cycle - during exercise.

28
Q

What kind of charge does Glutamate have ?

A

-ve charge

29
Q

What kind of charge does Alanine and Glutamine have and what does that mean with regards to membranes ?

A

No charge - easier to pass through membranes

30
Q

Where is excess Glutamate metabolized ?

A

The mitochondria of the hepatocytes

31
Q

What does Oxaloacetate get metabolized into once combined with alpha-ketogluterate in the Mitochondria ?

A

Aspertate

32
Q

What is the first Nitrogen Acquiring reaction in the Mitochondria ?

A

Glutamate -> Carbomyl Posphate

33
Q

What does Carbomyl Phosphate turn into before it leave the Mitochondria ?

A

Citruline

34
Q

What also leaves the Mitochondria to meet up with Citruline in the Cytoplasm and what does this create ?

A

Aspertate meets with Citruline in the cytoplasm to form Arginosuccinate & this is the 2nd nitrogen acquiring reaction

35
Q

What is the order of events from Arginosuccinate to urea production ?

A

Arginosucinate -> Arginine -> H2O = Urea

36
Q

What are the two broad classes of Amino Acid ?

A

Glucogenic and Ketogenic

37
Q

What do Glucogenic amino acids generally go on to become ?

A

Oxaloacetate -> Glucose

38
Q

What do Ketogenic amino acids generally go on to become ?

A

Ketone Bodies

39
Q

How many disorders of the urea cycle are there ?

A

there are 6

40
Q

What is the most common disorder of the urea cycle ?

A

The most common is an ornitine transcarbamoylase (OTC) deficiency.

41
Q

What is the purpose of OTC ?

A

Turns Ornitine back into Citruline in the urea cycle

42
Q

How is OTC deficiency inherited ?

A

It is an x linked inheritance

43
Q

How is OTC deficiency usually characterized ?

A

By hyperammonaemia (abnormally high levels of ammonia in the blood) which can be toxic

44
Q

In what age bracket does OTC deficiency usually present ?

A

New born

45
Q

In which cycle is OTC deficiency disorder found ?

A

The urea cycle

46
Q

In amino acid disorders decreased enzyme activity will do what to the product and the precursors ?

A

Decrease the product and increase the precursors

47
Q

What is one of the most common amino avid disorders ?

A

Phenylketonuria (PKU)

48
Q

How is PKU defined ?

A

as an absence or deficiency of Phenylalanine Hydroxylase (PAH)

49
Q

What is the purpose of the enzyme PAH ?

A

It catalyses the reaction of Phenylalanine to Tyrosine

50
Q

What occurs in this pathway when PAH is not present ?

A

There is a build up of Phenylalanine and Phenylalanine turns into Phenylpyruvate and then phenylacetate

51
Q

What occurs in an individual who has not been treated for PKU ?

A

Impaired brain development

52
Q

How is PKU treated ?

A

Decreased amounts of dietary protein and tyrosine supplements

53
Q

What is generated from Tyrosine ?

A

Thyroxine & L-DOPA

54
Q

When is PKU usually first spotted in babies ?

A

Once they start feeding phenylalanine levels will rise

Science for Medicine (18 decks)

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