Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

(1) KCU COM: SFM > Quiz 1 (Protein/AA Metabolism) > Flashcards

Quiz 1 (Protein/AA Metabolism) Flashcards

1
Q

Defective transport of nonpolar/neutral amino acids, especially ____, can lead to ____ Disease.

A

Tryptophan / Hartnup

*key characteristic = photosensitivity

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

Defective transport of dimer is cystine and dibasic amino acids can lead to ___.

(What are theses amino acids?)

A

Cystinuria

*key characteristic = cystine crystals in the kidneys causing abdominal pain

(“COLA” - Cystine / Ornithine / Lysine / Arginine)

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

Essential Amino Acids

A

“TIM HRKL VolsWagon Ferrari”

Or

“My Tall Handsome Vegan Friend Is Reliably Watering Kale Leaves”

Methionine (M) / Threonine (T) / Histidine (H) / Valine (V)/ Phenolalanine (F) / Isoleucine (I) / Arginine (R) / Tryptophan (W) / Lysine (K) / Leucine (L)

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

Alpha-ketoglutarate can act as a precursor for the synthesis of which amino acid(s)?

A

Glutamate

*Glutamate —> Glutamine / Histidine / Proline / Arginine

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

Pyruvate can act as a precursor for the synthesis of which amino acid(s)?

A

Valine / Alanine* / Leucine

*directly

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

OAA can act as a precursor for the synthesis of which amino acid(s)?

A

Aspartate* / Asparagine / Lysine / Methionine / Threonine / Isoleucine

*directly

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

3-Phosphoglycerate can act as a precursor for the synthesis of which amino acid(s)?

A

Serine* / Cysteine / Glycine

*directly

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

Exopeptidases attack the ____ of a protein.

Endopeptidases attack the ____ of a protein.

A

Exo- = C- and N- terminus ends

Endo- = digestive (specific) sites within the protein

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

Lysosomes sequester Intracellular proteolytic enzymes that are active when ___.

A

pH = 5

*because the lysosome creates a low pH environment, these enzymes are active within the lysosomes, but not outside them (where pH =7)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

The catalytic core of a proteosome is termed as the ___ subunit.

A

20S

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Ubiquitin receptors in the ___ regulatory unit of a proteosome target multi-Ubiquitin chains.

A

19S

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

Cleaving of peptide bonds in a proteosome is made possible by ____ which acts as a nucleophile.

A

-OH of Threonine

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

Trypsinogen, an inactive zymogen, is activated by an ___ that is embedded in the intestinal mucosa.

A

Enterokinase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What role do enteropeptidases play in protein digestion?

A

They convert the zymogen trypsinogen to active trypsin

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

Ketogenic / Glucogenic Amino Acids

A

Ketogenic (only) = Lysine / Leucine
*form precursor for ketone bodies or fatty acids (Acetyl-CoA or Acetoacetate)

Both = Phenolalanine / Tryptophan / Tyrosine / Isoleucine / Threonine
*”FWY IT”

Glucogenic = all others
*form precursors for glucose metabolism

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

What are the 3 main steps in amino acid metabolism?

A
  1. Aminotransferase / Transaminase = shuffling of amine groups
  2. Glutamate Dehydrogenase
  3. Urea Cycle = repackaging and excretion of amine group as ammonium
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

___ is the ketoacid of aspartate.

A

OAA (Oxaloacetate)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Transaminase reaction require the use of the coenzyme ___ which is a derivative of ___.

A

PLP (pyridoxyl-5’-phosphate)

Vitamin B6

19
Q

Transamination reaction transfer amino groups to ___.

A

Alpha-keto acids.

20
Q

Glutamine Synthetase converters Glutamate to Glutamine in order to trap ___.

A

Nitrogen

*for later excretion in the Urea Cycle

21
Q

Met, Thr, Ile, and Val can be metabolized to form ___ which can be converted to ___ (an intermediate of the TCA cycle).

A

Propionyl CoA

Succinyl CoA

22
Q

Mutations in ___ are the most common cause of homocystinuria.

A

CBS (cystathione beta-synthase)

*enzyme used in the metabolism of Methionine

23
Q

Deficiencies in pathways for metabolizing branched chain amino acids results in ___.

What are these amino acids?

A

Maple Syrup Urine Disease
*usually caused by deficient activity of BCKD complex

Val / Ile / Leu

24
Q

Phenylalanine metabolizes into ___ by the enzyme ___.

A

Tyrosine

Phenylalanine Hydroxylase
*if defective, leads to Phenylketonuria (neurological problems / musty urine)

25
Q

Hypothyroidism vs. Hyperthyroidism

A

Hypo- = low T4 / high TSH

Hyper- = high T4 and T3 / low TSH

*T3 and T4 (thyroxine) are made by Thyroglobulin which consists of Tyrosine resides

26
Q

Key amino acid derivative:

Tyrosine —> ?

Serine —> ?

Glutamate —> ?

Tryptophan —> ?

A

Tyrosine —> thyroid hormones (T3/T4); endocrine hormones (dopamine); melanin

Serine —> Acetylcholine (involved in neurotransmission)

Glutamate —> GABA

Tryptophan —> Serotonin (which is converted to Melatonin); NAD+ and NADP+ (requires Vitamin B6)

27
Q

Grave’s Disease results from defective metabolism of ___.

A

Tyrosine

28
Q

Albinism is a result of the inability of ____ to be converted to melanin, resulting in a lack of pigmentation.

A

Tyrosine

29
Q

Ammonia is removed as ___ and ___ in the brain.

A

Glutamate / Glutamine

*other tissues: Alanine / Glutamine

30
Q

What occurs when there is excess ammonium?

A

Glutamate Dehydrogenase will continue to generate glutamate from alpha-ketoglutarate to use up the NH4+

This lowers the pool of alpha-ketoglutarate, which lowers TCA cycle activity, learning to unconsciousness

31
Q

Pyruvate is the alpha-keto acid of ___.

A

Alanine

32
Q

The urea cycle primarily takes place in the ___.

A

Liver

33
Q

An Alanine Aminotransferase (ALT) is used in the removal of excess NH4+ from the ___.

A

Muscle

34
Q

Reactions of ALT and GLDH

A

ALT - transamination
*transfer of NH3 onto Glutamine

GLDH - oxidative deamination
*generation of NH4+

35
Q

What is the rate limiting enzyme of the Urea Cycle?

A

Carbamoyl Phosphate Synthetase

36
Q

Urea production is ___ by a high protein diet and ___ by a high carb diet.

A

Increased / decreased

*proteins tend to bring in amino acids with Nitrogen

37
Q

A defect in ___ can cause hyperammonemia since ammonium ions cannot enter the Urea Cycle.

A

CPS-1 (Carbamoyl Phosphate Synthetase)

38
Q

Ammonia (NH3) is a toxic agent while ammonium (NH4+) is not because…

A

As an uncharged molecule, ammonia can permeate/cross membranes and cause pH imbalances leading to swelling of cells

39
Q

Creatine is made from which 3 amino acids?

A

Arg / Gly / Met

40
Q

___ serves as a diagnostic for myocardial infarction.

A

CK-MB (creatine kinase)

41
Q

Basic essential amino acids:

A

His / Lys

42
Q

Branched chain amino acids are initially metabolized in the ___ because the enzyme ____ is in higher concentration there.

A

Muscles / branched-chain amino acid transferase

43
Q

Urea is synthesized in the liver from ___ and ___.

A

Aspartate / Carbamoyl Phosphate

(1) KCU COM: SFM (8 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions