Protein And Amino Acid Metabolism Flashcards
What happens to excess amino acids in the body
Cannot be stored so used for fuel
Kwashiorkor
Protein deficiency but adequate calories
Famine edema
Inadequate synthesis of plasma proteins like albumin so fluid Escape into tissues (oncotic pressure)
Marasmus
Protein calorie deficiency
Starvation
People at risk of protein malnutrition
Pregnant and lactating women
individuals with eating disorders
chronic alcoholics
substance abusers
hospital patients with major protein
needs
elderly
clinical chronically ill
individuals patience with genetic disorders in amino acid metabolism
Essential amino acids (PVT TIM HALL)
Phenylalanine
Valine
Tryptophan
Threonine
Isoleucine
Methionine
Histidine
Arginine
Leucine
Lysine
Is arginine always an essential amino acids
No
essential in children because of active growth but nonessential in adults
What is a glucogenic Amino acid
Product can enter gluconeogenesis
What is a ketogenic amino acid
Product intermediate of lipids metabolism or Ketone bodies
Positive nitrogen balance
More intake than excretion
Growth, pregnancy, tissue repair
Negative N balance
N excretion > intake
Starvation
Malnutrition
Illness
Surgery
General rédaction of amino acids
Transamination
Oxidative deamination
Decarboxylation
Transdeamination
Transamination
Caralyzed by transaminases (aminotransferase)
Transfer of NH2 to produce another AA
Co factor of transaminases
Pyridoxal phosphate from vit B6
Main compound in AA metabolism
Glutamate
Glutamine
a-KG
Neutral transport and storage form of ammonia
Glutamine
Glutamate dehydrogenase rxn
a-KG ——-> glutamate by glutamate dehydrogenase
Glutamate ——> glutamine by glutamine synthétase
Glutamine —-> glutamate by glutaminase
Genetic disorder in which glutamate dehydrogenase always activated due to binding site of GTP mutation
Hyperinsulinism - hyperammonemia syndrome with hypoglycemia
Where in the body do you find amino acids oxidase
The kidney
Decarboxylation of AA
Removal of CO2 by glu decarboxylase to form GABA
Transdeamination
Coupling of aminotransferase
with glutamate dehydrogenase reaction ( transamination+ deamination )
Tryptophan metabolized to
97%: Alanine Acetyl Coa CO2 Formate
3% :
Melatonin
Serotonin
Nicotinate ( niacin )
Serotonin function
Neurotransmission Behavioral processes (!appetite, agression , sleep ,sensory perceptions, depression Vasoconstriction Regulate circadian cycle , intestinal peristalsis
Agonist of serotonin
LSD
Antidepressants and their MOA
Paxil
Prozac
Zoloft
Inhibits serotonin reuptake
Hartnup disease
Defect in transportation or absorption of amino acids in intestine
Leads to essential amino acid deficiency and nicotinamide deficiencies
Hartnup disease symptoms
Hereditary pellagra like skin rash
Temporary cerebellum ataxia
Renal amino aciduria
Hartnup disease 3 D’s
Dermatitis
Diarrhea
Dementia
What factors precipitate hartnup disease
Sunburn Fever Inadequate nutrition Irregular diet Stress
Under what form is NH3 excreted
Urea
Direct sources of ammonia in liver
Glutamate
Glutamine (extrahepwtic tissues )
Alanine (muscles )
Organs that contributes the most to waste nitrogen
Muscles
Allostérie activator of CPSI
N acetylglutamate
Difference between CPSI and CPSII
CPSI only in mitochondria and uses NH3 in urea cycle
CPSII only in cytosol and uses glutamine in pyrimidine synthesis