Nitrogen Flashcards
State the main nitrogen-containing molecules of the body
proteins, nucleic acids, nucleotides, biologically active amines, haem-containing molecules
Describe the fate of dietary proteins
dietary protein is digested to produce amino acids for use in anabolic pathways
dietary proteins are enzymatically hydrolysed
Describe the flow of nitrogen through the body
digestion of dietary protein
‘turn-over’ of body protein
excretion of nitrogen as urea
maintenance of a pool of intra- and extra-cellular free amino acids
Describe the role of glutamate in transfer of nitrogen to, from and between amino acids
Nitrogen is transferred to, from and between amino-acids by oxidative deamination and transamination (aminotransfer) reactions involving glutamate
Glutamate is the only amino- acid that can obtain its nitrogen directly from ammonium ions
Describe the catabolism of body protein
gastric glands in stomach lining - pepsin cuts protein into peptides in the stomach
Trypsin and chymotrypsin cut proteins and larger peptides into smaller peptides in the small intestines
amino peptidase and carboxypeptidase A and B degrade peptide into amino acids in the small intestine
villus, intestinal mucosa absorb amino acids
Describe how nitrogen is transported through plasma to the liver
Nitrogen from turned-over body protein is transported through plasma to liver as glutamine, or, from skeletal muscle, as alanine
Transport of potentially toxic ammonia in large amounts is avoided
Describe the formation of urea
is a metabolite (breakdown product) of amino acids
when the liver breaks down protein or amino acids, and ammonia
Excess ammonium ions are converted to urea in the urea cycle
Describe the fate of the carbon of catabolised body protein
Carbon of turned- over amino-acids may be used to form intermediates of glycolysis, gluconeogenesis, citric acid cycle or lipid metabolism pathways
Carbon of amino-acids metabolised to pyruvate or citric acid cycle intermediates may become carbons of glucose: such amino-acids are called ‘glucogenic’
Amino-acids providing acetyl Co A or acetoacetate carbon atoms are called ‘ketogenic’
Describe examples of how metabolic defects in the urea cycle give rise to clinical problems
Rare group of inherited metabolic disorders - 6 inherited disorders of the urea cycle
- most common = omithine transcarbamcylase
(OTC) deficiency -1 in 40000 births in UK
OTC has x-linked inheritance, rest are autosomal recessive
characterised by hyperammonaemia (elevated blood ammonia levels) - highly toxic - medical emergency
typically present in newborn babies
Describe the Urea Cycle
cycle is split between mitochondria and cytosol, 5 enzymes catalyse cycle in the liver and their concentrations increase or decrease in response to high or low protein diets
CP51 is regulatory enzyme -(carbamoyl phosphate synthase) - Acetyl-glutamate is allosteric activator of CP51
Describe Phenylketonuria
absence/ deficiency of phenylalanine hydroxylase (PAH) - classical PKU
autosomal recessive disorder
associated with increrased phenylalanine (PHe) levels -toxic - due to no breakdown by PAH
untreated individuals exhibit signs of impaired brain development
treatable condition - reduced protein diet supplemented with tyrosine