ENZYMES Glyceraldehyde 3-phosphate dehydrogenase.

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Presentation transcript:

ENZYMES Glyceraldehyde 3-phosphate dehydrogenase

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

Orotidine-P decarboxylase OMP UMP +CO2

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: 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)