nitrogen metabolism (deev- only one question) Flashcards

1
Q

What is one of the most abundant porphyrin rings in the body?

A

Heme

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2
Q

____________ is most abundant but is too inert for use in most biochemical reactions.

A

Atmospheric nitrogen (N2)

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3
Q

True/False: Humans store nitrogen in the Liver.

A

False, we have no storage from of Nitrogen!

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4
Q

True/False: Nitrogen is a reactive compound.

A

True, most explosives contain nitrogen, so the body needs to get rid of any nitrogen that is above the needs.

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5
Q

Most nitrogen leaves the body via the _______ cycle.

A

Urea, clears body of excess nitrogen, but also retains carbon skeltons

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6
Q

How does nitrogen enter the body?

A

Most nitrogen enters in amino acids by digestion

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7
Q

What are 3 ways to input AAs?

A

Dietary protein (Digestion)
Protein turnover
amino acid synthesis de novo (from scratch)

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8
Q

What are 3 ways to output AAs?

A

Synthesis of proteins- Transcription, translation
Synthesis of other nitrogen containing compounds (nucleotides, heme)
Use of Carbon skeleton of AA for other compounds (i.e. glucose, lipids, ketone bodies) or for energy.

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9
Q

Input and output of AA is always balanced, why?

A

If you don’t have a certain amino acid in the body, certain proteins can’t be made…

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10
Q

What selectively degrade damaged or short-lived proteins, uses ubiquitin to target proteins for degradation? What energy does it use?

A

Proteasomes

Energy dependent mechanism—uses ATP

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11
Q

What non-selectively degrades intracellular proteins (autophagy) and extracellular (heterophagy)?

A

Lysosomes

use acid hydrolases to brake down peptide bonds to short peptides and AA

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12
Q

Enzyme in stomach?

A

Pepsin

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13
Q

Small intestine enzymes?

A

Pancreatic enzymes- trypsin, chymotrypsin, elastase, Carboxypeptidase
Aminopeptidases, Di- and Tripeptidases

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14
Q

All enzymes cleave specific sequences of amino acids via 2 enzymes.

A

Endopeptidases - inside a peptide sequence

Exopeptidases- from the ends (exo) of a peptide sequence

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15
Q

Peptides are hydrolyzed to amino acids in the ______.

A

Cytosol

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16
Q

Only free amino acids are found in the ________ after a meal containing protein.

A

portal vein

17
Q

Branched chain amino acids are not metabolized by the liver, instead sent from liver primarily to _____ via blood.

A

Muscle

18
Q

What is the first step and what enzymes are involved in the removal of Nitrogen from Amino Acids? What is the name of the step?

A

Step 1: Transamination, aminotransferase

transfers AA to alpha ketogluterate producing alpha keto acid.

19
Q

What is the 2nd step and what enzymes are involved in the removal of nitrogen from amino acids? Where does this occur?

A

Step 2: Oxidative deamination, Glutamate dehydrogenase

Occur in Liver and Kidney

20
Q

What are the sources of ammonia?

A
Dietary AA
Glutamine
Bacterial action
Amines
Catabolism of purines and pyrimidines
21
Q

Ammonia is constantly produced in the ________ but is present at very low levels in blood.

A

tissues

22
Q

_________ is highly neurotoxic and must be kept at low levels in the blood

A

Ammonia

23
Q

Any free ammonia present in the circulation will be removed by the ______, and used for synthesis of ___.

A

Liver

Urea

24
Q

Free ammonia is released in the _____ and contributes to the acid-base balance of the body by excreting protons.

A

urine

25
Q

What is a general term for elevated levels of ammonia in the blood, which can be due to many different conditions.

A

Hyperammonemia

26
Q

Elevated ______, above 1000 micromol/l, ________ intoxication is a medical emergency and can have effects on the CNS/ blurring of vision

A

ammonia

ammonia

27
Q

A disease that is due to a deficiency in cystathionine synthase. Promotes damaging of LDLs and dislocation of the lens can occur.

A

Homocystinuria in the urine

28
Q

A defect in enzymes involved in the conversion of tyrosine to melanin will cause _______.

A

Albinism

29
Q

Most severe form of albinism is the deficiency in the enzyme ______ and results in a complete lack of pigment.

A

tyrosinase