Biochem Test Iv: Amino Acid

Front 1

Why do we measure serum albumin levels?

Back 1

Albumin is made by the liver. We measure because if they are low it means that the liver is not getting enough essential amino acids.

Front 2

Where do we store amino acids?

Back 2

in our blood

What do we do if we run out of an essential amino acid?

Hint 2

we have to breakdown skeletal muscle to get it.

Front 3

which is smaller. amino acid storage pool or glucose storage pool (glycogen)?

Back 3

Amino acid storage pool

Front 4

What are the three reasons for 300 g of protein turnover each day?

Back 4

1. To prevent accumulation of abnormal proteins
2. To allow rapid changes in protein concentration (rate limiting enzymes)
3. To have a readily available source of amino acids.

Front 5

What are the 9 major functions of amino acids?

Back 5

1. Heme- RBC
2. Choline - PL
3. Glucosamine- Amino sugar
4. Nucleotides- DNA
5. PROTEIN SYNTHESIS- Protein 75%!!!
6. Biogenic amines - Neurotransmitters
7. Carnitine - Heart function
8. Creatine Phosphate
9.Detox in liver

Front 6

What are the 4 systems we use to breakdown protein?

Back 6

1. Lysomal (cathepsins) (extracellular protein)
2. Calcium dependent (calpains) (intra-cellular protein)
3. Ubiquitin-proteasome dependent (Intra-cellular protein)
4. Caspases- used for apoptosis

Front 7

What is a protease?

Back 7

any enzyme that can hydrolyze protein

Front 8

Which of the four systems that are used to breakdown protein, accounts for the most protein breakdown?

Back 8

Upiquitin-proteosome. accounts for nearly 80%

Front 9

What two enzymes protect us by trapping amonia?

Back 9

Glutamate dehydrogenase (Mito)
Glutamine synthestase (Mito and Cytoplasm)

Front 10

Is glutamate dehydrogenase a reversible enzyme?

Back 10

no

Front 11

What are the 4 metabolic classifications of amino acids?

Back 11

Essential, nonessential, glucogenic, ketogenic

Front 12

Which AA are Ketogenic?

Back 12

Leucine and Lysine

Front 13

What are the 8 Essential AA?

Back 13

GE: Methionine, Threonine, Valine
GKE: Isoleucine, phenyl-alanine, tryptophan
KE: Leucine, Lysine

Front 14

How many essential AA are there?

Back 14

8

What are the two ketogenic AA?

Hint 14

Leucine and Lysine

Front 15

Which amino acid is the GKN?

Back 15

Tyrosine

Front 16

Can we synthesize lycine or leucine?

Back 16

No.

Can we get glucose from them?

Hint 16

no

Front 17

What is the precursor we use to make alanine?

Back 17

Pyruvate

Front 18

What is the precursor we use to make glutamate?

Back 18

a-KG

Front 19

What is the precursor we use to make aspartate?

Back 19

oxalacetate

Front 20

What is the precursor we use to make serine?

Back 20

3PG

Front 21

What is the precursor we use to make asparagine?

Back 21

aspartate

Front 22

what are the two options we have for removing the Alpha-amino group off of the Amino Acid?

Back 22

1. Transamination reaction
2. Oxidative deamination

Which one produces Ammonia?

Hint 22

Oxidative deamination

Front 23

Which amino acids can not be transaminated?

Back 23

lysine, Threonine, proline, hydroxyproline

Front 24

Which vitamin does transamination require?

Back 24

B6

Front 25

What two enzymes are used to form ammonia?

Back 25

Glutamate dehydrogenase
D and L Amino acid oxidase (2 for each amino acid)

Front 26

What happens to the Nitrogen in Transamination?

Back 26

its just moved around, its never released as amonia

Front 27

Will a B6 deficiency increase or decrease ammonia production?

Back 27

increase

Why?

Hint 27

because transamination requires B6, so if you don't have it, you are left with oxidative deamination which produces ammonia.

Front 28

What enzyme forms the ammonia that the liver uses for urea formation?

Back 28

Glutamate Dehydrogenase

where is this enzyme located?

Hint 28

Mitochondrial Matrix

Highest activity in liver, but all tissues have it

Front 29

What are the two main carriers of nitrogen in the blood?

Back 29

Alanine and Glutamine

Front 30

Where does the liver get the nitrogen used to form ammonia?

Back 30

from alanine and glutamine

Front 31

What cleaves glutamine and what does it form?

Back 31

Glutaminase cleaves glutamine to form glutamate and get ammonia.

Front 32

Is Alanine transaminated to get nitrogen into glutamate?

Back 32

yes

What does it break alanine into with ALT?

Hint 32

forms pyruvate and glutamate

Front 33

Where does the Nitrogen in Urea come from?

Back 33

1 from glutamic Acid and the other comes from Aspartatic Acid

Front 34

Are transaminase reactions reversible?

Back 34

yes

Front 35

What is the rate-limiting enzyme for the urea cycle?

Back 35

CPS-1 (Carbamoyl Phospate Synthetase I) located in the mitochondria

What regulates this enzyme?

Hint 35

CPS-I is dependent upon N-Acetylglutamate for activity

Front 36

What does N-acetylglutamate do?

Back 36

regulates CPS-I which is the rate limiting enzyme of the urea cycle

What does it take to make it?

Hint 36

Acetyl-CoA and glutamate
catalyzed by N-acetylglutamate synthase

Front 37

How can we make the urea cycle turn over faster?

Back 37

have excess proteins coming in or we are in the fasting(starvation) state

Front 38

Where is the urea cycle found?

Back 38

only in the liver

Where is the rate limiting enzyme found?

Hint 38

in the mitochodrial matrix

Front 39

What can you use to get rid of nitrogen in individuals with a genetic defect in a urea cycle enzyme or who has liver failure

Back 39

Benzoate and phenylacetate infusion can be used to help remove nitrogen

Front 40

Does Alanine stimulate N-acetylglutamate synthase?

Back 40

yes

Front 41

Alanine works on Nacetylglutamate synthase which makes acetylglutamate which acts on CPS-1?

Back 41

yes