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FATE OF AMINO GROUP I. DEAMINATION A. Transamination by Aminotransferase (or Transaminase) Funnel -amino groups from a variety of AAs to glutamate by reacting with ketoglutarate.
amino acid + -ketoglutarate -keto acid + glutamate Does not result in any net deamination.
B. Oxidative Deamination
1. Glutamate Dehydrogenase (in mitochondria) See p.692 Glu + NAD+ (or NADP+) + H2O NH4+ + -ketoglutarate + NAD(P)H +H+
An enzyme unusual (but not the only one as stated in the Textbook) in being able to use NAD+ and NADP+. Plays a central role in AA metabolism. In most organisms glutamate is the only AA which has such an oxidative deamination enzyme. Glutamate DH is allosterically regulated. It is inhibited by GTP and ATP, and activated by GDP and ADP. The NH4+ so obtained can feed into urea cycle. 2. L-Amino Acid Oxidase Requires FAD as a cofactor.
D-Amino acid oxidase also exists in mammalian tissues. Real physiological function unknown.
C. Direct Deamination of Serine and Histidine 1. Serine Dehydratase Fig. 20-15. PLP-dependent serine + H2O pyruvate + NH4+ 2. Histidine Ammonia Lyase Fig. 20-17, Reaction 8. histidine urocanate + NH4+
UREA CYCLE
1932 by Hans Krebs and Kurt Henseleit as the first metabolic cycle elucidated. See Fig. 20-9. Overall Reaction: NH3 + HCO3 + aspartate + 3 ATP + H2O urea + fumarate + 2 ADP + 2 Pi + AMP + PPi Requires 5 enzymes: 2 from mitochondria and 3 from cytosol.
4. Argininosuccinase (Cytosolic)
5. Arginase (Cytosolic)
Only the ureotelic animals have large amounts of the arginase. arginine + H2O urea + ornithine
2. All other urea cycle enzymes are controlled by the concentrations of their substrates.
Deficiency in an E (substrate) rate of the deficient E.