Date post: | 20-Dec-2015 |
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Glyceraldehyde 3-phosphate dehydrogenase
ENZYMES
Protein structure overview
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
Structure is everything!!!!!!!
Burg-Waechter.de
OMP
UMP +CO2
Orotidine-P decarboxylase
Working with enzymes makes you really happy!
Leonor Michaelis Maud Menten
Michaelis-Menten diagram with inhibitor and activator
Competetive inhibition
Non competetive inhibition
Lineweaver-Burk equation
-Double reciprocal plot of linear transformation of MM equation
-Y-intercept 1/Vmax
- X-intercept -1/Km
Inhibition of enzymatic reactions
competetive
uncompetetive
Non-competetive
Optimal conditions for enzymatic reactions
Temperature: optimal reaction temperature depends on environment (Thermophilus aquaticus, ice fish)
pH:amylase in the mouth (spit) peptidases and proteases in stomach
Co-factorsProstetic 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)