3. Fig. 23-1, p.630 Amino acids act principally as the building blocks and to the synthesis of variety of other biologically molecules. When a.acids deaminated (removed the α- amino group), their C-keletons can be fed to TCA cycle. They may be used as precursors of other biomolecules.

4. How are amino acids synthesized?  The α-amino group of glutamate and the side-chain amino group of glutamine are shifted to other compounds: transamination reactions  The biosynthesis of amino acids involves a common set of reactions Reductive amination Amidation

5.  Glutamate is formed from NH 4 + and α- ketoglutarate in a reductive amination that requires NADPH. This reaction is catalyzed by glutamate dehydrogenase (GDH)  The conversion of Glutamate to Glutamine is catalyzed by glutamine synthetase (GS) that requires ATP  Combination of GDH and GS is responsible for most assimilation of ammonia into organic compound. However, the K M of GS is lower than GDH

6. Fig. 23-6, p.635

7. Transamination reactions: Role of Glutamate and Pyridoxal phosphate Amino acids biosynthesis

8.  Enzyme that catalyzed transamination require pyridoxal phosphate as coenzyme

9. Fig. 23-8b, p.637

10. Fig. 23-9, p.638

11. One-C transfer and the serine-family  In amino acid biosynthesis, the one-C transfer occurs frequently  E.g serine family (also include glycine and cysteine)  Ultimate precursor of serine is 3- phosphoglycerate (obtainable from glycolitic pathway)  The conversion of serine to glycine involves one- C unit from serine to an acceptor  This is catalyzed by serine hydroxymethylase, with pyridoxal phosphate as coenzyme  The acceptor is tetrahydropholate (derivative of folic acid) – its structure has 3 parts: a subtituted pteridine ring, p-aminobenzoic acid and glutamic acid

13. Fig. 23-12, p.641 Serine + tetrahydrofolate → Glycine + methylenetetrahydrofolate +H 2 O

14. Fig. 23-13, p.641 The conversion of serine to cysteine involves some interesting reactions In plants and bacteria: serine is acetylated to form O-acetylserine (by serine acyltransferase, and acetyl-CoA as acyl donor)

15. Fig. 23-14, p.641

16. In animals: the reaction involves the amino acid methionine Methionine (produced by reactions of the aspartate family) in bacteria and plants can be obtained from dietary sources – essential amino acids

17. Fig. 23-16, p.642

18. Table 23-1, p.643 What are essential amino acids? The biosynthesis of proteins requires the presence of all 20 amino acids If one is missing or in short supply, the protein biosynthesis is inhibited Protein deficiency will lead to the disease kwashiorkor; severe in growing children, not simply starvation but the breakdown of the body’s own protein

19. Catabolism of amino acids  In catabolism, the amino nitrogen of original amino acid is transferred to α-ketoglutarate → glutamate, leave behind the C skeletons  Disposition of C skeletons There are two pathways of the breakdown of C skeletons depends on type of end product: i. Glucogenic amino acid: yields pyruvate and OAA on degradation (can be converted to glucose with OAA as intermediate) Ii. Ketogenic amino acid: one that breaks down to acetyl-CoA or acetoacetyl-CoA to form ketone bodies

20. Table 23-2, p.644

21. Fig. 23-17, p.644  Excretion of excess nitrogen  Excess nitrogen is excreted in one of three forms: ammonia, urea and uric acid  Animal in aquatic env.: release as ammonia  Terrestrial animal: urea (soluble in water)  Birds: uric acid (insoluble in water)

22.  Urea cycle  Central pathway in nitrogen metabolism  The nitrogen that enter urea cycle come from several sources  A condensation reaction bet. ammonium ion and CO 2 produce carbamoyl phosphate in a reaction that requires of two molecules of ATP/carbamoyl phosphate

23.  In human, urea synthesis is used to excrete excess nitrogen, after consuming a high- protein meal  The pathway is confined to the liver  The synthesis of fumarate is a link bet. the urea cycle and TCA cycle

24. p.646a

25. p.648 When amino acid catabolism is high, large amounts of glutamate will be present from degradation of glutamine, from synthesis via glutamate dehydrogenase and from transamination reaction. Increase glutamate level leads to increase levels of N-acetylglutamate followed by increasing the urea cycle activity.