生物化学资料：氨基酸的脱氨基作用.pptVIP

Deamination of amino acid Transamination Oxidative deamination Transdeamination Overview Transamination : the funneling of amino groups to glutamate The first step: the transfer of their α-amino group to α-ketoglutarate The catabolism of most amino acids α-keto acid glutamate Oxidative deamination As an amino group donor Aminotransferases (transaminases) The equilibrium contant is near 1 !!! Aminotransferases Location: cytosol and mitochondria of cells throughout the body Substrate specificity α-ketoglutarate The acceptor of the amino group Mechanism of action of aminotransferases coenzyme a derivative of vitamin B Diagnostic value of plasma aminotransferases Normally intracellular enzymes Liver disease Nonhepatic disease In the liver and kidney mainly α-keto acids and free ammonia Glutamate dehydrogenase Enter the energy metabolism A source of nitrogen in hepatic urea synthesis NAD+ NADP+ (oxidative deamination) (reductive amination) Low energy lever High AA degradation??? Coenzymes Direction Allosteric regulators Let’s see the process D-Amino acids are in plants and cell walls of microorganisms D-Amino acids in the diet can be metabolized by kidney and liver DAO is a FAD-dependent peroxisomal enzyme the oxidative deamination of the AA isomers can produce α-keto acids, ammonia ,and hydrogen peroxide Transdeamination(Main way) Transdeamination: the combined actions of transamination and the oxidative deamination of glutamate by which the amino groups of most amino acids can be released as ammonia. Purine Nucleotide cycle (another Transdeamination ) myocardium skeletal muscle L-glutamate dyhydrogenase low activity L-glutamate dyhydrogenase Transdeamination Key enzyme:adenylate deaminase(腺苷酸脱氨酶) AMP can deaminize catalyzed by adenylate deaminase. transdeamination Purine Nucleotide cycle Non-oxidative deamination 1. Dehydration＆deamination： 2.Hydrogen sulfide removal＆ deamination ： 3.Direct deamination： Serine dehydrase Ammonia+pyruvate Ser