Flashcards in Metabolism - Amino Acid Metabolism Deck (22)
What are the essential amino acids?
What amino acids may become essential under certain conditions?
What is the nitrogen balance in health, starvation and pregnancy?
Health - 0 N balance
Pregnancy - + N balance
Starvation - - N balance
How much protein does the average person carry?
6kg which holds ~ 100000kj energy
How is nitrogen taken in, used and lost in the body?
Taken in via diet
Used to form N compounds (a/a, bases) and proteins
Lost via hair, nails a s as waste products in the urine.
How is protein broken down?
Protein to amino acids.
Amino acids to amino group and C skeleton
C skeleton to products for gluconeogenesis or ketone body formation.
How can amino groups be removed in protein metabolism?
1). Transamination - the amino group is transferred to a keto acid
--> ALT (alanine aminotransferase) converts alanine to glutamate (uses alphaketoglutarate)
--> AST (aspartate aminotransferase) converts glutamate to aspartate (uses oxaloacetate)
2). Deamination is the removal of the amino group to form NH3, which is then converted to NH4+
--> NH4+ is toxic so needs removing via conversion to glutamine or urea.
Where does the urea cycle occur and how many enzymes does it require?
What a the basics of the urea cycle?
Glutamate is converted to aspartate and fed into the cycle. 2ATP, CO2 and NH3 are also fed in from the mitochondrial matrix. Urea is produced.
What are the effects of complete/partial loss of an enzyme in the urea cycle?
Complete = fatal.
Partial = hyperammonoemia and accumulation/excretion of the product. Leads to the symptoms of NH3 toxicity (vomiting, blurred vision, tremor, coma) and is managed by a low protein diet with amino acids replaced by keto acids.
Where is ammonia produced?
Why is ammonia toxic?
It has pH effects (alkali)
Affects neurotransmitter synthesis
Reduces TCA activity by reacting with alpha-ketoglutarate = produces glutamate and disrupts energy supply to cell.
How does the body detoxify ammonia?
NH3 + ATP + glutamate ----> glutamine
Glutamine is used to synthesise N containing compounds
Released from cells and transported via blood to:
Kidneys for excretion
Liver to be put into urea
Where it is broken back into ammonia by glutaminase.
What is happening in phenylketonuria?
1). Phenylalanine hydroxylase is missing = can't convert phenylalanine to tyrosine = no dopamine, adrenaline or noradrenaline can be made.
2). Takes alternative pathway to give phenylpyruvate.
= phenylalanine and phenylpyruvate build up
Why is the build up of phenylpyruvate and phenylalanine a problem in phenylketonuria?
Phenylpyruvate - inhibits uptake of pyruvate into mitochondria so glucose isn't metabolised well = brain damage as brain can only use glucose.
Phenylalanine - competes with other a/a to use the transporter to cross the blood brain barrier = starves brain of others = mental retardation.
How is phenylketonuria treated?
Diet low in phenylalanine
What parts of the body does homocystinuria affect and why?
The CVS, CNS, CT and muscles as it affects fibrillin1
What cofactors does the enzyme CBS require?
What happens in homocystinuria?
1). CBS enzyme is missing so which normally produces cystathionine and therefore cysteine.
2). Homocysteine therefore enters another pathway which requires VitB12 and produces methionine.
= methionine and homocysteine build up
What damage does homocysteine and methionine build up in homocystinuria cause?
Methionine - competes with other a/a to cross blood brain barrier of brain = mental retardation
Homocysteine - binds to Lys residues in fibrillin1 protein, altering the proteins shape. This gives certain characteristics:
-lens dislocation in eye
What gas signalling molecules are produced during amino acid metabolism and what are their roles?