1. ENZYMES
Glyceraldehyde 3-phosphate dehydrogenase

2. Protein structure overview

3. Enzymes as biological catalysts
Enzymes are proteins
Enzymes reduce the activation energy of a single and specific chemical reactions
active site/unique surface structure
Enzymes are not altered by the reaction
Enzymes are biological catalysts. They stabilize the transition state from substrate to product
Many enzymes use co-enzymes (co-factors) to achive maximum activity.
metal ions, vitamins

4. Structure is everything!!!!!!!
Burg-Waechter.de

7. Orotidine-P decarboxylase
OMP
UMP +CO2

8. Working with enzymes makes you really happy!
Leonor Michaelis
Maud Menten

9. Michaelis-Menten diagram with inhibitor and activator

10. Competetive inhibition

11. Non competetive inhibition

12. Lineweaver-Burk equation
Double reciprocal plot of
linear transformation of MM equation
Y-intercept 1/Vmax
X-intercept -1/Km

13. Inhibition of enzymatic reactions
competetive
uncompetetive
Non-competetive

14. Optimal conditions for enzymatic reactions
Temperature:
optimal reaction temperature depends on
environment (Thermophilus aquaticus, ice fish)
pH:
a-amylase in the mouth (spit)
peptidases and proteases in stomach
Co-factors
Prostetic groups: heme, flavin, iron-sulfur groups
metal ions, (Mg2+ DNA polymerase)
Coenzymes: (vitamins), CoenzymeA (acyl groups),
NADH (dehydrogenase) – NAD- (reductase)
ATP (Kinase) – ADP (phosphatase)
SAM (S-adenosyl methionine) (ACC synthase)