Protein metabolism Flashcards

1
Q

Protein digestion & absorption (overview)

A

Stomach - proteins to polypeptides (HCL, Pepsin)

Pancreas (peptidases)

SI - polypeptides to amino acids (peptidases

absorbed as amino acids

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2
Q

What happens to amino acid pools

A

constantly synthesises into body proteins and then broken down again

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3
Q

what happens to excess amino acids

A

made into CHO or Fat

amine group comes off and is excreted as urea through urine/sweat

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4
Q

Amino acid structure

A

C H O N w/ specific R group

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5
Q

What effect does increase insulin have on amino acids

A

It arrives at the liver and is synthesised into protein and transport to tissues or is stored as CHO/Fat

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6
Q

What happens to amino acids when fasted (catabolic)

A

Amino acids/proteins broken down (amine group removed) to give CHO for energy

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7
Q

How do proteins enter the TCA cycle (ketogenic & Glucogenic)

A

Ketogenic - made into acetyl-CoA

Glucogenic - feed into all different parts of the cycle depending on the AA

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8
Q

name of AA wo/ nitrogen group (amine)

A

Alpha keto - acids

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9
Q

What does Transamination do

A

Transfers amino group from AA to alpha ketoacid in the presence of a transaminase

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10
Q

Why is transamination important

A

needed for non essential amino acid production in body - & is reversable

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11
Q

where does transamination occur

A

most tissues including muscle

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12
Q

2 common transamination examples

A

Alanine + a-Keto glutamate = pyruvate + Glutamate

Aspartate + a-Keto glutamate = oxaloacetate + Glutamate

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13
Q

why is alanine transamination important during exercise

A

can be transaminated into pyruvate in liver for energy

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14
Q

why is aspartate transamination important

A

for urea cycle function

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15
Q

How does oxidative deamination work

A

ammonia group is removed

eg Glutamate to A-ketoglutarate

Is reversible & dependant on substrate availability/requirements

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16
Q

where does oxidative deamination occur

A

in the mitochondria matrix of the liver

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17
Q

Why is Glutamine synthesis important

A
  • Has 2 nitrogen’s (can remove 2 ammonia groups at once)
  • the most abundant free AA in blood
  • Gluconeogenic precursor
  • Fuels GI & immune systems
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18
Q

How is nitrogen (ammonia) removed from the body

A
  • small amounts are excreted rest enters the urea cycle (energy & enzyme regulated)
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19
Q

AA - Urea link

A

^ AA = ^ Urea

Flux is dependant on substrate supply

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20
Q

How does the urea cycle work (carbamoyl production)

A

Ammonia + Co2 = Carbamoyl phosphate (enzyme = carbamoyl phosphate synthetase)

Irreversible

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21
Q

How does the urea cycle work (the cycle)

A

Carbamoyl phosphate combined with aspartate to produce urea - uses energy (fumarate side product for TCA cycle)

Urea out via sweat/urine

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22
Q

Branched chain amino acids (BCAA) examples & importance

A
  • Leucine, Isoleucine, Valine

Can be oxidised in skeleton muscle mitochondria

important for muscle protein synthesis

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23
Q

BCAA oxidation overview

A

each pathway is specific w/ enzymes

Vitamin B12 and biotin required in pathways

Products are fed into TCA cycle

24
Q

How does glycogen get back into the blood from muscle (Glucose-Alanine cycle work)

A

Glycogen -> G-6-P -> Pyruvate -> Alanine (transamination) -> released by muscle into blood

25
What happens to alanine once in the blood (Glucose-Alanine cycle work)
enters the liver and undergoes transamination w/ a-ketoglutarate forming pyruvate and glutamate Pyruvate undergoes gluconeogenesis producing glucose
26
What happens to glucose/glutamate produced in the liver (Glucose-Alanine cycle work)
Glucose - it is release back into the blood and transported to muscle/brain Glutamate deaminated (ammonia excreted)
27
Muscle protein synthesis definition
Building up of amino acids into functioning muscle
28
Muscle protein breakdown definition
Degradation of polypeptide chains within a muscle
29
net balance definition
relationship between synthesis and breakdown
30
Turnover defintion
constant use and restoration of protein
31
Protein synthesis (PS) - protein breakdown (PB) = ?
net protein balance
32
PB > PS = ?
negative protein balance (protein loss)
33
PS > PB = ?
positive protein balance (protein gain)
34
What % of basal energy expenditure is used for RNA formation
20%
35
why do some proteins have short half-lives
enzymes only needed for a short period of time
36
What does selective gene expression do
determines structural and functional characteristics of various cell types
37
How do genes & proteins differ
genes may be expressed but proteins must be activated, modified or converted
38
Protein synthesis process order
- transcription - translation - post translational modification & protein activation
39
Transcription process overview
copying DNA strand to mRNA (complementary base pair) Enzyme = RNA polymerase
40
How is transcriptional controlled (3 groups)
Activators - bind to enhancer sites promoting transcription Coactivator proteins - correctly position RNA polymerase Repressors - bind to silencer sites
41
How is RNA polymerase regulated?
general factors - set base rate specific factors - interact to modulate rate hormones - specific (steroids) - modulate process - Secondary messenger (cAMP) - bind to cell membrane
42
What does aminoacyl tRNA synthetase do?
catalyses binding of AA to appropriate tRNA (w/ ATP) is able to proofread before releasing tRNA
43
3 steps of translation
Initiation Elongation Termination
44
What is translation initiation
40S + 60S ribosomal subunits + mRNA molecule building new DNA molecule (signally proteins eg eIF2 control this process)
45
Common start and stop codons
Start - Met | Stop - Aug
46
What is translation elongation
adds AA to carboxyl terminal end of PP chain (because anticodon of aminoacyl-tRNA recognises second codon on mRNA) Peptide bond forms
47
What is translation termination
When a stop codon is reached a release factor releases the complete PP chain from the last tRNA (addition of water) ribosomal units separate
48
what do the 3 tRNA sites do (A P E)
A - landing site P - Second binding site E - Exiting site
49
what does post-translational modification do
- Continue folding to make the protein functional | - Transportation
50
What do molecular chaperones do
help build protein 3D shape (eg heat shock proteins HSP)
51
What do scaffolding proteins do
take proteins across mitochondrial membrane
52
Why do we breakdown proteins
Quality control - remove mutants, damaged Turnover - short life, not required Provision of AA - energy (a-ketoacids) , protein synthesis
53
How does Ubiquitin-proteosome breakdown proteins
marks a specific protein for degradation
54
How doe lysosomal breakdown proteins
endocytosis
55
How does caspases breakdown proteins
programmed cell death
56
how does matrix metalloproteinases
removes extracellular matrix breakdown proteins
57
Why is calpain used to breakdown protein in muscles
because it is calcium activated