Lesson 3: Enzymes Flashcards
enzymes
biocatalysts that accelerate metabolic reactions to biologically useful rates. They do this by lowering the activation energy. It is regenerated after the reaction.
substrate
what binds to the enzyme
Enzyme substrate complex
what enzyme and substrate are called put together
Transition state
substrate (bound to enzyme) becomes more reactive and the metabolic reaction accelerates.
Energy of activation
the energy needed to form the transition state
Active site
site intended for a substrate that is unique to a protein’s structure. Very complex and usually binds only one type of substrate.
denature
any structural change in an enzyme will destroy its effectiveness and will slow the reaction rate
Optimal conditions
range of values for environmental factors (temp, pH) that are ideal for enzyme
Temperature and enzymes
high temp increases the reaction rate only to a certain point where denaturing will occur after that.
pH and enzymes
acidic and basic solutions will interact with the r groups of the enzymes and can denature the active site. Many function best at 7 pH
Competitive Inhibitors and enzymes
molecules structurally similar to the substrate compete for a position at the active site of the enzyme. This inhibits the reaction
iodine turns what colour in the presence of starch
turns black
what causes breakdown of starch?
alpha amylase enzyme
effect of temp on hydrolysis
low temp has low enzyme activity as it reduces the kinetic energy of molecules, which gives fewer collisions between the active site with sufficient activation energy to allow reaction to pass transition state/ too high temp is denaturing
effect of pH on hydrolysis
acidic and basic solutions will interact with the r groups of the enzymes and can denature the active site. Many function best at 7 pH
effect of enzyme concentration on hydrolysis
more enzyme is faster hydrolysis
effect of heavy metal ions on hydrolysis
they are non-competitive inhibitors. reduces enzyme activity by altering the ability of the active site/ you can tell because the enzyme activity in the metal test tubes is slower than the control tube
noncompetitive inhibitor
does not look similar to the substrate but alters the shape of the active site which impacts binding of the substrate
figure statements
state the experiment and what is going on
how to do the hydrolysis graph
time is on the y axis, the variable is on the x axis and it is TOTAL TIME
optimal conditions
range of values for environmental factors (temp, pH) that are ideal for enzyme
