生物化学甲课件-史锋之Aminoacidoxidation.pptVIP

Amino Acid Oxidation and the Production of Urea Amino acids can be used as fuels in animals (especially in carnivores) Dietary proteins are enzymatically degraded to amino acids Enzymatic digestion begins in stomach and ends in small intestine Pepsin cleaves polypeptides into smaller peptides in stomach (N-term of Y, F, W); Trypsin and chymotrypsin further cleave the peptides in small intestine; Carboxypeptidase and aminopeptidase cleave the small peptides into amino acids, which are then absorbed and eventually delivered to liver. Amino acids in excess can neither be stored, nor excreted, but are oxidized as fuels Amino groups are separated from the carbon skeletons at the beginning The amino group is reused or excreted (as ammonia, urea or uric acid); The carbon skeletons (a-keto acids) generally find their way to the citric acid cycle for further oxidation or conversion. Most of the amino acids are metabolized in the liver: the amino groups are delivered from extrahepatic tissues to liver via Glu or Gln a-ketoglutarate collects the a-amino groups from many amino acids Aminotransferases (transaminases) catalyze these transamination reactions to form Glu and a-keto acids; All use pyridoxal phosphate (PLP，吡哆醛磷酸) as the prosthetic group; Reactions are freely reversible. PLP covalently binds to the enzyme and transiently carries an amino group PLP is derived from pyridoxine (vitamin B6); PLP binds to the enzyme via covalent and noncovalent bonds; The aldehyde form and aminated form(pyridoxamine) of the prosthetic group can easily interchange, taking or releasing an amino group. The transamination reaction via PLP takes a ping-pong mechanism One amino acid transfers its amino group to PLP and then departs the active site as an a-keto acid; Another a-keto acid moves in and takes the amino group from pyridoxamine phosphate and leaving as an amino acid (Glu). Glutamate collects and delivers ammonia to the liver Glutamine synthetase catalyzes the addition of ammo