师兄考研生化下学期2biosynthesis of amino acids and related molecules.pptxVIP

Biosynthesis of amino acids and related molecules氨基酸及其衍生物的生物合成 ContentsOverview of nitrogen metabolismReduction (fixation) of N2 into ammonia (NH3 or NH4+)Synthesis of the 20 amino acidsSynthesis of other biomolecules from amino acids1.The nitrogen cycleNitrification硝化作用2. Nitrogen is fixed by enzymes of the nitrogenase (固氮酶) complexNitrogen fixation: Conversion of N2 to NH3 in diazotrophs (固氮生物) Cyanobacteria (蓝绿藻, photosynthetic) rhizobia (根瘤菌, symbiont 共生生物 )RhizobiaCyanobacteriaRhizobia exist innodules ofleguminous plantsAmmonia is incorporated into biomolecules through glutamate and glutamineFirst, glutamine synthetase (Gln 合成酶) catalyzed the reaction of glutamate and NH4+ to yield glutamine.Glutamate is produced from glutamine and α-ketoglutarate in a reaction catalyzed by glutamate synthase (Glu合酶).The amide group of Gln is the source of nitrogen in the synthesis of a variety of compounds, such as Trp, His, carbamoyl phosphate (氨基甲酰磷酸), glucosamine-6-P, CTP, and AMP.The amino groups of most other amino acids are derived from glutamate through transamination.Glutamine synthetase is a primary regulatory point in nitrogen metabolism The enzyme has 12 identical subunits (each having an independent active site forming two hexagonal rings ) and is regulated by both allosterically and by covalent modification.The bacterial Gln synthetasehas 12 subunits arranged as two rings of hexamersActivesites Tyr397(adenylylation site)Regulation by allosteric effectorsThe glutamine synthetase is accumulatively inhibited by at least 8 allosteric effectors, mostly end products of glutamine metabolismA specific Tyr residue (Tyr397) in bacterial glutamine synthetase can be reversible adenylylatedAdenylylated enzyme is more sensitive to the allosteric inhibitor (变构抑制剂).The addition and removal of the AMP group to the glutamine synthetase are catalyzed by adenylyltransferase (AT, 腺苷酰基转移酶).Activity of AT is modulated by binding to a regulatory protein, PII.The activity of PII, in tu