生物化学IILectureAmioacidcatabolism.pptVIP

Overview Amino acid oxidation Transamination and deamination Role of pyridoxal phosphate (PRPP) Urea cycle NH3 transport in body (gln, ala) NH3 ? urea Amino acid degradation – fate of carbon skeleton Example A: Thr, gly, ser, ala (tetrahydrofolate rxn) Example B: Phe, Tyr Example C: Val Diseases and disorders (some examples) Amino acid metabolism Amino acids are not stored like glucose or fatty acids Ie: no polymeric form dedicated for “reserves” of amino acids Only muscle provides any real source if not supplemented in diet Humans lost ability to synthesize 10 amino acids Most of them require complex pathways, lots of energy, lots of enzymes Why can’t we synthesize them? Evolutionary advantage? Excess amino acids cannot be stored and therefore are broken down Glycolysis/TCA cycle intermediates Amino acid oxidation Amino acids large source of energy Depending on animal can be as much as 90% (carnivores) Essentially 2 pathways to consider when breaking down amino acids: Fate of amino group Fate of carbon skeleton Transamination and Deamination Example of transamination Glutamate is always involved in transamination (aminotransferase) reactions. Many types of transaminases that are specific for a certain amino acid Coenzyme PLP (pyridoxal phosphate (Vit B6)) is required by all transaminases Pyridoxal phosphate Cofactor for all transaminase reactions Acts to transfer an amino group from an amino acid to a keto-acid Pyridoxal phosphate – rxn mechanism for transaminases NH4 transport and deamination The oxidation of amino acids leads to a buildup of glutamate (acceptor of NH3) Glutamine serves as the principle carrier (non-toxic) of excess NH4 in the blood Transported to liver (mitochondria) where it is processed: NH4 is removed Glu Dehase is an example of oxidative deamination Alanine as secondary NH4 carrier Alanine serves to transport NH4 from the muscle to the liver Formed by ala transaminase (seen previously) with glu as the NH4 donor Reverse reaction hap