biological molecules-enzymes Flashcards
what are enzymes
- globular proteins that catalyse metabolic reactions
- anabolic reactions: larger molecules are built up from smaller molecules
- catabolic reactions: larger molecules are broken down/hyrolysed
enzymes as biological catalysts
- catalyst: a molecule that speeds up a chemical reaction but remains unchanged at the end of the reaction
- enzymes are biological catalysts made of protein (speed up rate of a chemical reaction)
- requires in small amounts
- remain unchanged at the end of the reaction
- specific in action
- affected by temperature and pH
- enzymes are always present in cells and organisms but some are only produced under particular conditions/at certain stages (allows for cells to control what chemical reactions and when they happen in the cytoplasm)
- for reaction between 2 organisms to occur, there must be an effective collision between them for activation energy to be produced
- must collide with each other in right orientation and speed
metabolic reaction
for reaction to take place
- activation energy is needed to raise molecules to an unstable high energy intermediary state prior to formation of product molecules
(because of the extra energy within them, they become unstable)
- an energy barrier needs to be overcome before the reaction takes place thus enzymes lower the activation energy is needed to activate the substrate molecules
- enzymes are highly specific in their action: only catalyse 1 type of reaction due to the specific 3-dimensional conformation and distinctive chemical properties of the active site where the substrate molecule bind
lock and key hypothesis
enzyme: lock
substrate: key
- an enzyme binds its substrate molecule at its active site, forming the enzyme-substrate complex
- when an enzyme-substrate complex is formed, the energy level of the substrate is raised to a transition state before it breaks down to form its product with the enzyme remaining unchanged
summary:
- the shape of the active site of the enzyme is specific and complementary to the shape of the substrate. upon effective collision between enzyme & substrate, the enzyme-substrate complex is formed
- interactions between enzyme and substrate molecules strain/weaken chemical bonds within substrates, thus lowering activation energy
- when reaction between substrates finish, products no longer fit into active site and are released
factors affecting enzyme reaction
pH:
- all enzymes have optimum pH in which it functions most effectively
- at the optimum pH:
- all bonds within enzyme are intact (maintain its specific 3-dimensional conformation thus enzyme active site is complementary to its substrate)
- maximum number of enzyme-substrate complex to be formed per unit time, converting substrate to products
- changes in pH alter the enzyme bonding pattern (alters 3-dimensional conformation of the active site, substrate is no longer complimentary to the active site –> no enzyme-substrate complex–> no product formed–> thus enzyme is denatured and no product formed)
- effects of pH on active site is normally reversible if not too extreme (unlike temperature changes)
temperature:
- for every 10 degree celsius rise in temperature, rate of enzyme reaction is doubled until optimum temperature is reached
- as temperature increases, KE of substrate and enzyme molecules increase thus increasing the frequency of effective collisions between substrate and enzyme active site
- increases formation of enzyme-substrate complex
- increases rate of reaction/products formed
- enzyme activity is highest at 35-40 degree celsius
- when temperature exceeds optimum temperature of 40 degree celsius:
- high temperature breaks the bonds that hold enzyme active site in its functional conformation (enzyme is denatured–> loses catalytic function