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Transamination, Deamination,urea cycle 24-5-13 • Transamination & deamination reactions Transamination • α- ketoglutrate plays vital role in amino acid metabolism by accepting amino groups from most amino acids becoming glutamate • Glutamate become deaminated or used in the formation of non essential amino acids • location • exception of lysine & threonine Most important Amino Transferases • ALT: transfers amino group of alanine to alpha-ketoglutrate hence forming pyruvate & glutamate • AST: transfers amino groups from glutamate to oxaloacetate forming aspartate ( N source in urea cycle) • Plasma ALT, AST can be elevated in hepatic and non hepatic diseases i.e. Myocardial and muscle disorders • Deaminations Glutamate dehydrogenase causes the oxidative deamination of amino acids liberation free ammonia (NH3) • Glutamate ---the only amino acid that undergoes rapid oxidative deamination • NAD+ or NADP+ as a coenzyme • (GTP) is an allosteric inhibitor of glutamate dehydrogenase, whereas (ADP) is an activator • When energy levels are low in the cell, amino acid degradation by glutamate dehydrogen ase is high, facilitating energy production Urea cycle • first two reactions leading to the synthesis of urea occur in the mitochondria, whereas the remaining cycle enzymes are located in the cytosol • One nitrogen of the urea molecule is supplied by free ammonia, and the other nitrogen by aspartate Ammonia disorders • The two major causes of hyperammonemia (with its CNS effects) are liver disease and inherited deficiencies of enzymes (such as ornithine transcarbamolyase) in the urea cycle Overall stoichiometry of the urea cycle • Aspartate + NH3+ CO2+ 3 ATP + H2O → urea + fumarate + 2 ADP + AMP + 2 Pi + PP