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24 Cards in this Set

  • Front
  • Back
alanine is second
to glutamine in the ciruclating amino acid competition
function of alanine-glucose t
to transfer nitrogen from peripheral tissues to liver
alanine in peripheral
produces
pyruvate: carbon skeleton is recycles
ammonia: eliminated via urea cycle
Alanine Glucose I
in the muscle, glucose goes through glycolysis to produce to 2 pyruvate, making ATP for energy
Alanine Glucose II
2 pyruvate goes to 2 Lactate via lactate dehydrogenase producing NAD+
Alanine Glucose III
as pyruvate levels increase, alanine levels increase proportionately via ALT
ALT reactions
type of aminotransferase reaction
uses glutamate as amino acid donor
alanine aminotransferase
Pyruvate-->Alanine
coupled with alpha KG --> Glutamate
formation of alanine ways
1) alanine aminotransferase
2) protein degradation
Alanine Glucose IV
alanine is transported to the liver using the blood
Alanine Glucose V
liver reverses the ALT process
Alanine-->Pyruvate--> Glucose
pyruvate undergoes gluconeogenisis to prouduce energy
alanine glucose VI
side product is the production of urea which is elminated via the urea cycle
catabolism of alanine
ALT
reverse process produces pyruvate
happens in the liver
aminotransferase reaction
pyruvate is recycled (gluconeogenic)
when is pyruvate gluconeogenic
the catabolism of pyruvate produces Co2 and water via the TCA cycle using pyruvate dehydrogenase: happens when the energy charge is low
making of aspartate
aspariginase
occurs in the urea cycle
cytosolic reaction
asparagine --> aspartate
uses the hydrolysis of H20 --> NH4
AST
aspartate goes to oxaloacetate
with the coupling of alphaketoglutarate to glutamate (PLP)
second transamination reaction
common transamination reactions
1) AST - aspartate to oxaloacetate
2) ALT - alanine to pyruvate

both use the coupling of alpha ketoglutarate to glutamate
PLP
pyridoxal phosphate
alpha keto to l glutamate
requires vitamin B6
cofactor for all aminotransferases
vitamin B6
cofactor for all aminotransferases
two ways to produces glutamate
alpha ketoglutarate to glutamate

1) PLP
2) GDH
GDH
L glutamate---> alpha ketoglutarate
H20 --> NH4
NADP --> NADPH
or NAD--> NADH
occurs in liver/kidney
regulation of GDH
positive: ADP, GDP
negative: ATP, GTP high energy charge
making glutamine
L glutamate goes to L glutamine
via
glutamine synthetase
using addition of ammonia to carboxyl group
and ATP
ATPammonia-->ADPphosphate
catabolism of glutamine
via glutaminase
glutamine--> glutamate + NH3
hydrolysis of amide group
produces NH3+ which is sent to the kidney tubule to be excreted into the urine
what happens to the ammonia produced by GDH
diffuses into the lumen of collecting tubules as NH3
NH3 combines with protons to produce ammonium chloride
which acidifies urine
indicator of tissue damage
AST and ALT in blood
AST: cardiac tissue
ALT: in liver