1. Amino acid degradation
Title slide - amino acid metabolism

2. The fates of the amino acids
The fates of the amino acids. The green box amino acids are glucogenic while the red-boxed ones are ketogenic. Note that the colors are different from the Stryer illustration Fig the gluconeogenic ones are red and the ketogenic are yellow.

3. Fates of the nonessential amino acids.

4. Fates of the essential amino acids.

5. Glutamate dehydrogenase.

6. Pyridoxal phosphate structure; vitamin B6.

7. The structures of oxal, oxine, oxamine forms of vitamin B-6.

8. Bound to the enzyme as an aldimine with the epsilon amino acid of lys (K).

9. Transamination pairs amino acid and oxoacid.

10. Glutamate-pyruvate aminotransferase.

11. Detailed mechanism of pyridoxal phosphate-catalyzed reactions.

12. Serine dehydratase. The proton on the alpha C is removal and electrons can shift. Other groups can be removed -OH.

13. A coupled pair of aminotransferase reactions.

14. Different forms of pyridoxal phosphate during the reactions.

15. More different forms during the reactions.

16. The pathways converting alanine, cysteine, glycine, serine, and threonine to pyruvate.

17. Reactions of the glycine cleavage system.

18. Degradation pathways for arginine, glutamate, glutamine, histidine, and proline to alpha ketoglutarate.

19. The pathway of methionine degradation.

20. The pathway of lysine degradation in mammalian liver.

21. The pathway of tryptophan degradation.