1 / 40

Enzymes: Basic Principles

Enzymes: Basic Principles. SBS017 Basic Biochemistry Dr John Puddefoot J.R.Puddefoot@qmul.ac.uk. Objectives: . To introduce the basic concepts and definitions of enzymology You should be able to able to define the terms Enzyme, Specificity and Co-factor

herman
Download Presentation

Enzymes: Basic Principles

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript


  1. Enzymes: Basic Principles SBS017 Basic Biochemistry Dr John Puddefoot J.R.Puddefoot@qmul.ac.uk

  2. Objectives: • To introduce the basic concepts and definitions of enzymology • You should be able to able to define the terms Enzyme, Specificity and Co-factor • You will understand the concept of Gibbs Free Energy and its relation to reaction equilibrium • You will be able to describe how enzymes effect the rate of biological reactions and be able to define • the term Activation energy in the context of Transition state theory .

  3. Enzymes • Biological catalysts • Almost all enzymes are proteins (but RNA can have enzymic activity too, “ribozymes”) • Function by stabilizing transition states in reactions • Enzymes are highly specific

  4. Enzymes accelerate biologicalreactions • e.g. Carbonic Anhydrase • CO2 + H2O H2CO3 • Each molecule of enzyme can hydrate 1,000,000 molecules of CO2 per second, 10,000,000 times faster than uncatalysed reaction

  5. Catalase 2H2O2 2H2O + O2

  6. Rate enhancement by enzymes • Kcat- maximum number of enzymatic reactions catalyzed per second.

  7. Enzymes are highly specificProteolytic enzymes

  8. Hydrolysis of esters

  9. Proteolytic Enzymes differ in degree of substrate specificity e.g Peptide bond hydrolysis (proteolysis) A. Trypsin cleaves only after arginine and lysine residues. B. Thrombin cleaves between arginine and glycine only in particular sequences. But Papain cleaves all peptide bonds irrespective of sequence

  10. Specificity is important e.g. DNA polymerase I • Adds nucleotides in sequence determined by template strand. • Error rate of < 1 in 1,000,000 • Due to precise 3D interaction of enzyme with substrate

  11. Major classes of enzymes

  12. Many enzymes require cofactors • Cofactors are small molecules essential for enzyme catalysis Can be: • Coenzymes (small organic molecules) • Metal ions

  13. Holoenzymes • Enzyme without its cofactor “apoenzyme” • With its cofactor “holoenzyme” • Cofactors are essential for activity e.g. many vitamins are cofactors, many diseases associated with vitamin deficiency due to lack of specific enzyme activity

  14. Enzyme cofactors

  15. Energy transformation • Many enzymes transform energy into different forms • Adenosine Triphosphate (ATP) is universal currency Light ATP Photosynthesis Food ATP Respiration ATP work

  16. ATP is an energy carriere.g. • ATP provides energy to pump Ca2+ acrossmembranes

  17. Free energy • The free energy of a reaction is the difference in free energy between its reactants and its products This called the ΔG • If ΔG is negative, the reaction will occur spontaneously “exergonic” • If ΔG is positive, energy input is required “endogonic”:

  18. Endergonic reactions ………………… ΔG is positive ……………………………………………………………………..

  19. Exergonic reactions …………………………………………………………………….. !G negative • ΔG is negative …………………

  20. Exergonic reactions H2O2 ΔG is negative 2H2O2 + O2

  21. ΔG is independent of reactionpath

  22. A system is at equilibrium and no net change • can occur if ΔG is zero

  23. Calculating ΔG • The free energy of a reaction is given by: Where: ∆G° is the standard free energy change (i.e. change at 1M concentrations), R is the universal gas constant T the absolute temperature

  24. Calculating ΔG at pH7 (ΔG’) • At equilibrium and standard pH 7 And so

  25. Calculating ΔG at pH7 (ΔG’) • Rearrange and substitute K’eq • or in log 10 • Rearranges

  26. Example • Calculate ΔG and ΔG°’ • At equilibrium GAP to DHAP is 0.0475 + 7.53 kJ mol-1

  27. If DHAP is 2 x10-4 M and GAP is 3 x 10-6 M -2.89

More Related