Amino Acid Metabolism II Flashcards

1
Q

Describe the 3 pathways that are used to synthesize amino acids and the pathways that they are related to

A

3-phosphoglycerate, phosphoenolpyruvate and pyruvate from glycolysis

alpha-ketoglutarate and OAA from the TCA cycle

Ribose-5-phosphate, erythrose-5-phosphate from the pentose phosphate pathway

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are the 3 transamination reactions that occur in amino acid syntheses

A
  1. pyruvate/alanine by SGPT
  2. OAA/Aspartate by SGOT
  3. alpha ketoglutarate/glutamate exchange by Glutamate dehydrogenase
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are the fates of aspartate and what enzymes catalyzes these reactions?

A
  1. Asparagine synthetase changes the molecule into asparagine
  2. In other organisms, Aspartate can be turned into lysine, methionine and threonine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Describe the fate of glutamate?

A

Glutamine synthetase forms glutamine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the difference between synthetases and synthases?

A

Synthetases use ATP and synthases do not

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Describe the regulation of glutamine synthesis

include what protein is involved

A

Adenylation (AMP addition) of the glutamine synthetase inactivates the enzyme

PII is a protein that binds to the adenylyl transferase, which causes adenylation of the enzyme (inactivation)

If a UMP is aded to the PII protein via uridylylation, and that binds to the adenylyl transferase, then the enzyme is deacetylated and the enzyme is activated

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Why is it important that the cells are able to make glutamine from glutamate?

A

So that the excess NH4+ can be transported to the liver so that it can go through the urea cycle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What are the amino acids that can be formed from glutamate?

A

Glutamine, Proline, and Arginine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What are the amino acid derivatives of 3-phosphoglycerate?

A
  1. three reactions get to serine
  2. vitamins B6 and B12 help to remove the side chains from serine to make glycine
  3. serine can be converted through cysteine via a homocysteine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is tyrosine a catabolic intermediate of?

A

Phenylalanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q
Where are aromatic amino acids derived from? And which intermediates from this pathway make 
Histidine 
Tryptophan 
Phenylalanine 
Tyrosine
A

Aromatic amino acids come from the pentose phosphate pathway

Histidine comes from ribose-5-phosphate

tryptophan, phenylalanine and tyrosine come from Erythrose 4 phosphate combining with phosphoenolpyruvate to make choorismate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

List and describe the amino acids that are synthesized from pyruvate?

A

Valine, Leucine, and Isoleucine

All have complex syntheses, exist to be incorporated into proteins, and are regulated by feedback inhibition

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

List the uses of amino acids

PAN

A

All Planning Parents Perform Active Sex Regularly—Now Pregnant

Activated Carriers 
Polypeptides 
Precursors 
Pigments 
Antioxidants 
Signaling Molecules 
Regulatory molecules 
Neurotransmitters 
Polyamines
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are the two central amino acids?

A

Glycine and Serine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Describe Heme

A

Acetate is converted to succinyl CoA prior to assembly

used for O2 transport

Heme is the main source of dietary iron

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Describe the deficiencies in Heme synthesis

  1. What happens if there is a deficiency in a liver enzyme?

2/ A non-liver enzyme?

A

Porphyrias

  1. Sx related to pain and cardiac dysfunction
  2. non-liver; light sensitivity and altered skin pigmentation
17
Q

Describe aliphatic molecules. What happens if you change the ring?

A

They absorb light via the pi-orbitals.

if you change the ring, you change the wavelength that is absorbed and changes the color transmitted (our eyes only see the transmitted)

18
Q

What are the molecules that are derived from glutamate?

A

Glutathione-antioxidant
Polyamines-stabilize DNA
GABA- inhibitory neurotransmitter

19
Q

List and describe the two arginine derived molecules

A
  1. NO: free radical that is from NOS; tied to G-protein signal cascade; nitroglycerin releases 3 equivalents of NO
  2. creatine phosphate: liver releases into the bloodstream; hydrolysis of phosphate from creatine releases same amount of energy as ATP
  3. uses SAM (methyl donor) a TON
20
Q

What are the histidine derived molecules?

A

Histamine- secretion of HCl and pepsin in the stomach, vasodilation at the site of allergic reaction, neurotransmission

21
Q

What kind of inhibition do antihistamines use?

A

Competitive inhibition

22
Q

What are the tryptophan derived molecules?

A

serotonin; dictate insulin release from the pancreas, vasoconstriction and blood pressure regulator, intestinal contraction, NOS activation, and a precursor for melatonin

23
Q

Describe the tyrosine-derived molecules

A

Catecholamines:
epinephrine (stress hormone) that causes vascular constriction, increase in blood pressure, and ceases inflammation

dopamine: increased leads to drug addiction and parkinson’s, decreased levels in parkinson’s and ADHD

24
Q

Describe dark hair color

A

Eumelanins> phemolanins

25
Q

Describe light hair color

A

Pheomelanins> eumelanins

26
Q

What is albinism caused by?

A

A deficiency in tyrosinase