3.1.4.2 MANY PROTEINS ARE ENZYMES Flashcards
What are enzymes?
- biological catalysts:
- speed up the rate if reaction without being used up
- provide an alternate pathway with lower activation energy
Are enzymes globular or fibular proteins?
Globular proteins
What can enzymes be?
Intracellular/ extracellular
What are intracellular enzymes?
Produced and function inside the cell, made by free ribosomes
What are extracellular enzymes?
- Secreted by cells and catalyst reactions outside cells
- made by ribosomes on the RER (eukaryotes)
What is a catabolic reaction?
Involves the breakdown of complex molecules into simpler products:
- happens when a single substrate is drawn into the active site and broken apart into two or more distinct molecules
- e.g. cellular respiration and hydrolysis
What is an anabolic reaction?
- involves the building of more complex molecules from simpler ones by drawing two or more substrates into the active site forming bonds between then and releasing a single products
- e.g. protein synthesis + photosynthesis
What is the lock and key hypothesis?
The enzyme splits the substrate molecule into two smaller products, the enzyme can catalyse the reverse reaction
What is the induced fit theory?
- as substrate is bonding
- triggers a change in active site
- tertiary structure change in the active site shape
- breaks hydrogen bonds- enzyme fits substrate more closely to give the enzyme- substrate complex
6 Factors affecting rate of enzyme reaction?
- Temp
- PH
- Conc of enzyme
- Conc of substrate
- Inhibitors (competitive and non-competitive)
- Cofactors/ prosthetic group
What is the temperature, kinetic energy and collision theory?
- higher temp= higher KE
- more KE= more collisions
- more ESC’s form= more product forms
- rate of reaction increases
What is the Q10 theory?
- Q10 is the factor by which the rate of reaction increases for every 10 DC rise
- this is typically around 2, but varies between enzymes
What is protein denaturing?
Breaking of the bonds holding the enzyme’s tertiary structure in place:
- e.g. London bonds + hydrogen forces will be the first to go- resulting in the tertiary structure being disrupted and the active site changing shape
How could you change bonding in the enzyme to give greater thermostability?
Use stronger bonds such as covalent bonds:
- e.g. disulphide bridges
How to reduce the effect of a competitive inhibitor?
Add more substrate