energetics and enzymes Flashcards
enzyme catalysis: explain how enzymes act as catalysts of reactions. Draw graphs to show the effects of substrate concentration, temperature and pH on reactions catalysed by enzymes
define enzyme
protein acting as catalyst to induce chemical changes in other substances, but remains unchanged by process; increases rate or reaction; high specificity; delta G remains same but lowers Ea
hydrolase
catalyse hydrolytic cleavage
dehydrogenase
oxidise substrate by reducing coenzyme
protease
hydrolyse peptide bonds
nuclease
hydrolyse phosphodiester bonds
ligase
joins two molecules together
transferase
transfer functional groups
isomerase
rearrange bonds within molecule
polymerase
catalyse polymerisation reactions
kinase
catalyses phosphorylation and activation
phosphatase
hydrolytic removal of phosphate
oxido-reductase
one oxidised, one reduced (type of dehydrogenase)
ATPase
hydrolyses ATP
glucose-6-phosphatase
catalysed aq reaction of glucose-6-phosphate with water to form glucose and Pi
lysozyme: function
hydrolyses B(1-4) bond in peptidoglycan (NAG and NAM) so bacteria lyse and die
requirements of Glu-35 and Asp-52 to ensure maximum rate of lysozyme hydrolysis
Glu-35 is protonated and Asp-52 is ionised, so +ve transition can be stabilised
mechanism of Glu-35 and Asp-52
Glu-35 protonates the oxygen in the glycosidic link between the two sugars, breaking the glycosidic bond; water molecule enters and is deprotonated by Glu-35; Asp-52 stabilises the positive charge in the transition state; OH- attacks the remaining sugar molecule, adding an OH group to it; proton is transferred to Glu-35 to return it to it’s original state; Glu-35 and Asp-52 are both in their original state to continue catalysis
lock and key hypothesis
substrate shapes exactly complementary to active site
induced fit hypothesis
substrate induces change in active site (proteins possess degree of flexibility)
effect of pH on catalysed reactions
optimum pH, sharp decrease either side as enzyme denatures
effect of T on catalysed reactions
slow increase in rate as gain kinetic energy, optimum T, rapid decline as enzyme active site denatures
effect of [substrate] on catalysed reactions
increases until [enzyme] or other factors become limiting