Amino Acid Metabolism Flashcards
Metabolism (carbs, lipicds, proteins)
FAD > FADH2
NAD+ > NADH + H+
CO2 + H2O + ATP
Metabolism energy of proteins
dietary proteins
tissue proteins
amino acids metabolism depends on what?
depends on the energy requirements of the cell
amino acid degradation occurs under 3 circumstances depends on what body needs
we break down amino acids”
- protein turnover- break down our protein depends on diet
- protein rich diet- to much in body we break down what we dont use in body
- starvation, uncontrolled diabetes mellitus- dont have it so we use it as a fuel
amino acid supply:
where are amino acids stored?
not stored in the body
amino acid supply:
amino acids are not stored in the body:
dietary
synthesized
protein degradation
amino acid supply:
Excess amino acids are catabolized
Step 1: removal of amino group (nitrogen)
Step 2: carbon skeleton
what is the amino acid pool supplied by?
supplied by breakdown of endogenous protein dietary protein and synthesis of non essential AA
amino acid pool:
Free amino acids:
cells
blood
extrzcellular fluid
what is more abundant in the body proteins or free amino acids?
proteins are more abundant then Free Amino acids
What is the fate of amino acids?
Low energy charge
low glucose
high energy charge and lots of glucose
fates of amino acids and low energy charge
the amino acid is oxidized to recreate ATP
fates of amino acids and low glucose
the amino acids id sent to the liver to turn into glucose
fates of amino acids and high emergy charge and lots of glucose
the amino acid is sent to the liver and turned into fat
what can amino acids also be used to synthesize?
amino acids may also be used to synthesize protein or nitrogen containing compounds
Oxidation of amino acids means what?
means burning them in the aerobic system (krebs cycle and ETS) to get ATP
What oxidaizes most of the 20 amino acids in protein
the liver does
what can only oxidize significantly six?
muscle
When are amino acids oxidized?
when the cells’ energy charge is LOW
amino acid catabolism (alpha amino acids)
amino group - urea carbon skeleton (a keto acid) - ATP + CO2 + H2O - glucose -fatty acids
amino acid catabolism (alpha amino acids)
amino group - urea carbon skeleton (a keto acid) - ATP + CO2 + H2O - glucose -fatty acids
what is the primary site for uptake of most amino acids following a meal (50-60%)?
the liver
what are 20% used for? and where do they stay and released?
20% for synthesis of protein; most stay in the liver while the rest are released into the plasma
what are 20% used for? and where do they stay and released?
20% for synthesis of protein; most stay in the liver while the rest are released into the plasma
what is the 1st step in liver amicno acid metabolism?
where is it transferred?
step 1:
remove amino group: transmination (aminotransferase)
amino group transferred to a-ketoglutarate
glutamate and liver amino acid metabolism
amino group donor- bissynthetic pathways
excretion pathway of nitrogen
along with the liver what is also used in transamination?
peripheral tissues
where do most amino acids transfer their a-amino group to
to a a-ketoglutarate (amino group acceptor)
what are the results after the transfer of the a-amino group to the a-ketoglutarate?
results in glutamate and a an a-keto acid
what is the required conezyme for the transamination to happen?
pyridoxal phosphate (derivative of vitamin B6)
transamination:
amino acid to a
ketoacid uses aminotransferase
transmination:
a-ketoglutarate to
glutamate uses aminotransferases
alpha ketoacid:
a-amino acid to a ?
where is the amino group located here?
what is the carbonyl group associated with?
to a a-keto acid
amino group is on the alpha carbon
carbonyl group associated with the alpha carbon
what is left when the amino group is removed from an amino acid?
a-ketoacid is what is left
where is usually the amino group transferred to?
normally transferred to another a-ketoacid
where do ketoacids usually enter into metabolic pathways
krebs, gluconeogenesis, fat synthesis
what happens to an alpha keto acid depends upon what?
energy charge horomones (glucagon/insulin) respiratory quotient glucose concentraion tissue (liver vereus muscle)
what does every amino acid contain
an amino grouo (NH3)
what removes this amino group
amino acid catabolism removes this
what removes this amino group
amino acid catabolism removes this
where are most amino acids metabolized
in the lier
ammonia (NH3)
biosynthetic pathways
excreted
ammonia from extrahepatic tissues are transport where and then?
transport to liver (glutamate, alanine)
and excreted
what are the 4 amino acids in nitrogen metabolism?
glutamate
glutamine
alanine
aspartate
where can these amino acids in nitrogen ny easily converted to?
to krebs intermediates
glutamate to
a-ketoglutarate
glutamine to
a-ketoglutarate
alanine to
pyruvate
aspartate to
oxaloacetate
glutamate and a-ketoglutarate:
glutamine to glutamate by reduction of one (NH3)
glutamate to a-ketoglutarate (a ketoacid) by lose of (NH3 and gain of oxygen)
alanine and pyruvate:
alanine (AA) to pyruvate (a ketoacid)
aspartate and oxaloacetate:
Asparagine to asparate by reduction of one (NH3)
aspartate to oxaloacetate (a ketoacid) by lose of (NH3 and gain of oxygen)
glutamate and gluatmine collect?
collect amino acids
glutamate and gluatmine location? and transfer BLANK to BLANK?
liver;
amino acids tranafer their amino group to a-ketoglutarate to form glutamate
where does glutamate enters to release amino group and then forms NH4+
enters mitochondria
glutamate and gluatmine and extrahepatice tissues
ammonia generated in extrahepatic tissues is converted to glutamine
transported to the liver
both make up the highest concentration of amino acids in the liver
glutamate and gluatmine and extrahepatice tissues
ammonia generated in extrahepatic tissues is converted to glutamine
transported to the liver
both make up the highest concentration of amino acids in the liver
amino group have been collected where as ? is transported where from? amino groups are removed by?
collected in the liver as glutamate; glutamate is tranported to mitochondria from cytosol; amino groups removed by oxidative deamination
what is oxidative deamination? and provides what? for what cycle?
removal of amino groups as free ammonia; of glutamate in the liver provides amino group for the urea cycle
glutamate to what by what?
glutamate to glutomine + NH4+ by:
glutamatedehydrogenase (NAD+ > NADH) a-ketoglutarate
numerous transaminases are present to transfer the nitrogen to another molecule which will end up bringing it to the liver for deamination
skeletal muscle
glutamate to?
alpha KG