enzymes and nucleic acids Flashcards
describe the structure of enzymes
-tertiary proteins with globular shape
-has a pocket or cleft area which has a specific 3D shape called an active site where reactions take place
function of enzymes
-act as biological catalysts
-provide an alternate pathway during a reaction
-hydrolyse polymers into monomers in digestion
define biological catalyst
proteins that speed up metabolic reactions without being used up
how do enzymes lower activation energy?
by providing an alternate pathway during a reaction
what is the importance of the enzyme catalase?
-hydrolyses hydrogen peroxide into water + oxygen
-H202 is a toxic by-product of metabolism so must be removed
-catabolic
whats the importance of the enzyme RUBISCO?
-RuBP +CO2 into glycerate + phosphate
- fixes CO2 from atmosphere in photosynthesis
-anabolic
whats the importance of the enzyme ATPsynthase?
ADP +Pi into ATP
-energy requiring process
-active transport
-anabolic
whats the of the enzyme glycogen synthetase?
-converts glucose to a storage compound -glycogen (polysaccharide)
-anabolic
condensation
define activation energy
the extra energy that is required to enable a reaction to occur
where is the activation energy usually supplied through?
heat in a loboratory reaction
whats the importance of a model?
it provides simplified visual representations to explain how a process may work
describe the lock and key model of enzyme action
-specific active site is complementary to the substrate molecule so able to bind
-bonds broken
-2 products are formed
describe the induced fit hypothesis of enzyme action
-active site not fully complementary
-strain on bonds lowers activation energy
-the active site becomes complementary to the substrate
-an enzyme-substrate complex forms
-substrate no longer fits active site so products are released
what biochemical food test would determine if an enzyme was present?
-biuret solution (NaOH + CuSO4)
-blue to lilac
what factors may affect the rate of reaction of enzyme?
-pH
-temperature=Ke
-substrate concentration
-enzyme concentration
why will an enzyme only bind to one substrate molecule?
active site is only complementary to one type of substrate molecule
what is a limiting factor?
factors that effect maximum rate of reaction being achieved
explain how a very high temp can stop an enzyme from working?
-bonds will break
-active site denatures
-can no longer bind, no longer complementary to the substrate
-no enzyme-substrate complexes can form
explain how extreme pH can affect the overall shape of the enzyme
-hydrogen ions can interfere with R group interactions between amino acids as H+ will cluster around negatively charged R groups and disrupt the hydrogen and ionic bonds which maintain the tertiary structure of a protein and shape of active site
what is meant by the saturation point in an enzyme controlled reaction?
when all enzymes active sites are occupied
what is the limiting factor when increasing the substrate concentration?
enzyme concentration
explain the effect of temperature on enzyme activity
-as temp increases, the molecules have more kE
-more successful collisions between substrates and the enzymes active sites
-so more enzyme-substrate complexes
-so rate of reaction happens faster
-when the temp goes beyond optimum, H bonds break
-enzyme denatures + tertiary 3D structure of active site changes
-active site changes shape so more difficult to become complementary to the substrate
-so fewer to no enzyme-substrate complexes can form
-so rate of reaction slows down and stops
why are rate of reactions very slow at low temps?
enzymes and substrate molecules have little kinetic energy
and few enzyme-substrate successful collisions taking place
explain the effect of pH on enzyme activity?
-as the pH moves away from optimum, rate decreases
-because changes in pH changes charges on the R groups of the amino acids
-therefore this changes the ionic and hydrogen bonding
-therefore 3D tertiary structure of enzymes changes
-so active site denatures, no longer easy for active site to become complementary
-so fewer enzyme-substrate complexes can form
-so rate decreases then stops
what are the 2 main ways of measuring the rate of a reaction?
-start the reaction, then measure either the concentrations of product formed or substrate used up after a fixed time intervals
define initial rate
the rate of reaction is at its highest at the first few seconds beginning of the reaction when the conc of substrate molecule is highest and therefore more enzyme-substrate collisions so more ESCs formed
define v-max
point at which the reaction is fastest as all the enzyme active sites are occupied no more enzyme substrate complexes can be formed
formula for rate
1/time
explain the effect of increasing concentration of substrate on the rate of an enzyme catalysed reaction?
-if conc of enzymes remains constant and conc of substrate increases the number of collisions will increase
-more ESCs
-rate increases
-saturation point will be reached
-conc of enzymes active site limiting factor