1. Metabolic Biochemistry BIBC 102 Summer 2005

2. Lecture 1 August 1, 2005 Lehninger (4 th Edition), Chapter 3, 4, 6

3. Figure 4.2b

4. Figure 4.4a,b

5. Figure 4.4c

6. Figure 4.4d

7. Box 4-1

8. Figure 4.7a

9. Figure 4.7b

10. Figure 4.16 sperm whale myoglobin

14. hydrophobic side chains in blue

15. space filling model with atoms represented as spheres with van der Waals radii

16. Figure 4.23a deoxy-hemoglobin

17. Figure 4.24b

18. Macromolecular Museum

19. KEGG Kyoto Encyclopedia of Genes and Genomes

20. OMIM Online Mendelian Inheritance in Man

21. Chapter 6 ENZYMES

22. Enzymes are catalysts: speed up the reaction Enzymes have exquisite specificity: a) selection of substrates (chemical nature, stereochemistry) b)nature of the reaction catalyzed Enzyme activity can be regulated

23. Apoenzyme + Co-enzyme Co-factor Prosthetic group Metal ion(s) Active enzyme

26. The enzyme chymotrypsin with its active site and its substrate (red) LNC 6-1

27. LNC 6-4 Dihydrofolate reductase with the substrates tetrahydrofolate (yellow) and NADP + (red)

28. EC3.4.17.1: hydrolase - peptidase (subclass) - metallocarboxypeptidase (sub-subclass) - arbitrary assigned serial number NOMENCLATURE

29. page from KEGG Metabolic Chart

30. Regulation of enzyme activity 1.At the level of gene expression and protein turnover 2.By covalent modifications of side chains 3.By binding of small molecules (ligands) that are not substrates 5. allosteric mechanisms in multisubunit enzymes

31. ENZYME KINETICS LNC Chapter 6

32. REACTANTS SUBSTRATES PRODUCTS k First order reactions:A  P k Second order reactions:A + B  P

33. 1 st order:ln[A] = ln[A o ] - kt or [A] = [A o ] exp(-kt) 2 nd order: 1/[A] = 1/[Ao] + kt

34. TRANSITION STATE THEORY A C B D A C B D A C B D A catalyst serves in at least two ways: it binds and aligns the substrates it facilitates the redistribution of electrons (charges)

35. End of Lecture 1 August 1, 2005