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Metabolism Exam 3- Here we go!!Amino Acid Metabolism- Amino acids can either be synthesized in the body (endogenous) or obtained through the diet. Once you get them into the body they undergo anabolism in order to be synthesized for a variety of different bodily functions. Some significant functions are:o Hormones- insulin and glucagono Immunoproteins- antibodieso Biogenic amines- neurotransmitters Dopamine, epinephrine, and norepinephrine- Amino Acid Classification- by structure, net charge, and essentialityo Structure- Take a look at your online notes while I am explaining these Alipathic- This means non-polar hydrophobic. This group of hasside chains off of the base structure that consists of Carbon-Hydrogen only molecules. There is no net charge on the structures. Hydroxylic- This literally means a side chain with OH group in it.They are polar and can be somewhat hydrophilic with no net charge. Sulfur containing- These are the same as above, but with a S group and not an OH group Carboxyl or Amide- These are side chains that have either a COO- or amide group. These are hydrophilic amino acids. These tend to either have a net (-) charge (carboxyl) or no net (amide) charge Basic groups- These amino acids basically have another net + charge from an NH3+ somewhere in the side chain. Aromatic- These are simple, have an aromatic ring. The only significant one is Tyrosine. Tyrosine has an OH group, but it was derived from Phenylalanine so it takes priority. There is no net charge. Imino Acid- There is only one of these and it is Proline. Imino literally means have the N from the basic structure within the side chain, as you will see in the picture.o Net Charge- I mentioned how some of each structures have what net charge, but this is just to clarify a little and show what she said during class.  Zwitterions have none because the only charges is the + from the amino group and – from the carboxyl on the basic structure, they cancel each other out. So the Alipathic amino acids are great examples Polarity- This is the tendency for amino acids to interact with waterat physiological pH.- Can be classified as polar or non-polar depending on the side chain. I gave some examples when explaining structures.o Essentiality Non-essential- Endogenous- Alanine, Asparagine Aspartic Acid, Glutamic acid Essential- These are the ones that must be obtained from diet Conditionally essential- Usually not essential; illness or stress can cause the body toconvert non-essential to essential. o Met or Ser Cys o PheTyro Glutamate  Prolineo Glutamine or GlutamateArginineo Glutamate or AmmoniaGlutamine- Threonine, Histidine, or Lysine cannot undergo transaminationo Sources of Protein Exogenous- from food sources- Animal products- Anything except the fats. These are the best sources because they are complete. - Plant products- grains, legumes, and vegetables. These areincomplete so you have to eat all types to receive all amino acids Endogenous- from the body- Desquamated mucosal cells- body produces 50g/day- Digestive enzymes & glycoproteins- Body produces 17g/dayo Transamination- As I was saying before, certain amino acids do not undergo this.  It is the formation or non-essential amino acids from essential amino acids or to create another essential amino acids from anotheressential amino acid. It is usually the first step in any amino acid formation.  Catalyzed by aminotransferase enzymes which can be increased by cortisol.- Requires B6 as a coenzyme (PLP, pyidoxal phosphate)o PLP stimulates glucagon for protein breakdown  then the body can stress and cause cortisol to take the broken down protein (amino acids) and for glucose by cortisol.- Synthesis increases in the liver in response to glucocorticoids- Increased serum levels suggests liver damageo Alpha Keto Acid vs Amino Acid- On the alpha Carbon (the Carbon next to the COOH) there is a ketone on the Carbon to Keto Acid and a NH2 group on the alpha carbon of amino acid. o Ainotransferase reaction- This is the conversion of an amino acid to a keto acid.  Aminotransferase is the major enzyme PLP is the coenzyme Some examples:- Alanine can convert alpha keto acid  alpha amino acidby alanine amino-transferase (ALT). o This causes the Alanine  Pyruvate when transferring the amino acido Presesnt in the liver- Aspartate can convert alpha ketoacid to alpha amino acid by Aspartate amino transferase (AST)o This causes the AspartateOAA during the process. OAA can then enter the Krebb’s cycle. o Presesnt in the heart, but more in the liver.o Ammonia (NH3) Metabolism- This is the conversion of NH3 to make it nontoxic, organic linkages. There are 3 ways the liver can do this Reductive amination Production of amides- Glutamine and Asparagine Formation of carbamyl-PO4 (for urea synthesis and pyrimidine synthesis)o Glutamate Metabolism Aminotransferase (transamination) Oxidative deamination- Glutatmate is the only amino acid to undergo the oxidative deamination - This is glutamatealpha ketoglutarateo Glutatmate Dehydrogenase (reversible) o Hydrolysis (H2O in)o NH3 out to the Urea cycleo NAD+NADH + H+ Reductive amination- The reverse of above so alphaketoglutarate Glutamateo Same enzymeo NH4 in to form organic, non-toxic form (NEAA)o H20 outo NADPH + H+ NADP+ Formation of Glutamine- GlutamateGutamine. Glutamine is another way to get NH3 to a non-toxic form and is important for hormones in the enterocytes of muscles- Glutamine- Amide group so it has 2 amine groups- Glutamine Synthetase- irreversible step- ATP-ADP- NH4 in and H2O outo The Urea Cycle- Understand the Urea Cycle chart Arininosuccinate Synthetase- Major rate limiting enzyme The purpose for this cycle is converting NH3 to a non-toxic, excretory product (urea). Urea the major nitrogen source in urine. The process is located in the liver. - NH3 can be mad in the body by chemical reactions, food, and bacteria breakdown.  The disposal of ammonia can be done through- Kidney- excreted through the urineo 25% may be excreted into the intestinal lumen because of bacteria degredation- Regulation o Low protein diets- This causes you to have less excretion because you have less protein synthesis, meaning less Nitrogeno Increased metabolic acidosis- Causes more Urea disposalo Increased Starvation- Causes increased Urea disposal because your body is relying on glucagon which facilitates


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FSU HUN 3224 - Metabolism Exam 3

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