Help
Options
Didn't know it?
click below
click below
Knew it?
click below
click below
Don't Know
Remaining cards (0)
Know
retry
shuffle
restart
0:00
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
bio 3/4
structure and regulation of biochemical pathways
| Question | Answer |
|---|---|
| What is an enzyme? | Proteins that speed up specific reactions (catalysts) that binds to substrates to create the enzyme substrate complex. |
| What are the two ways enzymes can fit with the substrate? | Lock and Key method are when the active site and substrate fit together perfectly, and the induced fit model need the active site to have a conformational change in order for it to fit. |
| What is a biochemical pathway? | Sequence of reactions catalysed by different enzymes; product of each reaction becomes the substrate in the next reaction. |
| What is a catabolic reaction? | Breakdown of large molecules into smaller molecules creates an output of energy through breaking of bonds, and is an exergonic reaction. For example, aerobic and anaerobic respiration. |
| What is an anabolic reaction? | Builds a large molecule from smaller ones, input of energy as bonds are formed, and is an endergonic reaction. For example, photosynthesis. |
| What is irreversible inhibition? | Inhibitors with strong bonds with enzymes, denaturing of an enzyme by heat, changes in pH or other chemicals, and binding of poisons (eg. Some antibiotics bind irreversibly to bacterial enzymes). |
| What is reversible inhibition? | Bonds found between inhibitor and enzymes are weak (easily broken). |
| What is feedback inhibition? | When the amount of product is high, the pathway slows down (excessive product is inhibiting enzymes easily in pathways). |
| How does temperature affect the rate of enzymatic reactions? | Below enzymes optimum temperature (36-38 degrees), they do not function effectively. If it is above enzymes optimum temperature, the enzymes become inactivated and denature. |
| How does pH affect the rate of enzymatic reactions? | The availability of H+ ions can change ionic bonds that forms the tertiary structure of the protein. If pH is over optimal it will denature and the substrate will be unable to bind. |
| How does concentration of enzyme and substrate affect the rate of enzymatic reactions? | Increasing enzyme concentration will increase reaction rate, if you increase substrate concentration then the reaction rate will also increase. |
| What is a competitive chemical inhibitor? | A molecule that binds directly to the active site, blocking the substrate from binding, can be reversed. |
| What is a non-competitive chemical inhibitor? | A molecule that binds to an allosteric site of the enzyme, creating a conformational change in the enzymes active site, and the substrate cannot bind. |
| What are coenzymes? | A small, non-protein cofactor, most are carrier molecules such as NADH, NADPH and ATP that transfer elections to transfer energy. |
| How can coenzymes be loaded or unloaded? | Loaded forms means they are ready to donate a chemical group, proton or electron, ATP, . Unloaded forms means they are ready to accept a chemical group, proton or electron, ADP. They can be cyclically loaded and unloaded. |
Created by:
lucyokane
Popular Biology sets