Enzymes Flashcards
Significance of Vmax
Maximum rate of reaction, different for different enzymes and reflects their turnover number
Km
Gives you an idea of the efficiency of enzymes - higher turnover, higher Km
Half Vmax
Without enzymes
Most of body’s biochemical reactions would be too slow
Enzymes are proteins, identified using Biuret test (purple)
Enzymes
Speed up reactions without being changed at the end of the reaction
Only speed up 1 reaction as they are specific
Can be intracellular (DNA helical and DNA polymerase)
Or extracellular (digestive enzymes eg amylase that catalyse hydrolysis reactions)
Intracellular
Synthesised in the cell and work in the cell
Extracellular
Synthesised in the cell and works outside the cell
Zymase
First enzyme to be discovered, in yeast
Catalyses conversion of sugars to alcohol
Properties of enzymes
- generally work very rapidly
- not destroyed or used up by the reactions that they catalyse
- they are specific, work by the lock and key hypothesis so they are only found in small amounts inside cells
- proteins, and are chains of amino acids
- complex tertiary structure held together by hydrogen, ionic and disulphide bonds
- denatured by several factors including high temperatures and pH changes
Practical application
Catalase is an enzyme found in all living cells, and it speeds up the breakdown of hydrogen peroxide inside the cells to the products water and oxygen
Good sources of catalyse include liver, potato and celery
2H2O2 > 2H2O + O2
V fast turnover rate
Turnover rate
No substrate molecules converted into products
Reactions at low temperatures
Enzymes ensure reactions can happen at relatively low temperatures
They lower the activation energy of the reaction
Activation energy is the minimum energy required to overcome the repulsion between molecules
They do this by forming an E-S complexes and bending bonds
Formation of an enzyme-substrate complex increases the rate of reaction
Explain how
By lowering activation energy by bending bonds
Explain why maltase only breaks down maltose
Tertiary structure means the active site is complementary to maltose
Description of induced fit
Enzymes lower activation energy by forming E-S complexes
Once reaction is complete
The enzyme is free to bind with another molecule of substrate
Enzymes type
Globular protein with a complex tertiary structure
The combination of the enzyme with its substrate molecules is called an E-S complex and the part of the enzyme that fits with the substrate is called the active site