biolmol2 Flashcards
List all factors affecting enzyme activity.
Temperature, pH, [enzyme], [substrate], competitive and non-competitive inhibition.
How does temperature affect enzyme activity?
- Increased T = molecules have a higher KE.
- More successful collisions between enzymes and substrate per unit time - more E-S complexes formed per unit time.
- However, excessive vibration from high temperatures (usually 60+ degrees) can break bonds holding the enzyme’s tertiary structure together - denatured.
How does pH affect enzyme activity?
- Change in pH alters the charges on the amino acids that make up the enzyme’s active site - no E-S complexes can be formed as substrate can’t attach.
- Could cause the bonds maintaining the tertiary structure to break - i.e. interferes with the ionic bonds etc. in tertiary structure. This alters the shape of the active site and therefore prevents E-S complexes from forming.
How does [enzyme] affect enzyme activity?
- Increase in [enzyme] = increase in rate as more E-S complexes formed per unit time - more likely collisions between enzymes and their substrate per unit time.
- But if [substrate] is limited, there are enough active sites to accommodate all the available substrate molecules - no further increase in rate.
How does [substrate] affect enzyme activity?
Assuming a fixed [enzyme]:
- [Substrate] is steadily increased, the rate increased in proportion initially - limited number of substrate molecules for enzymes.
- More substrate added until Vmax (max rate) is reached - all active sites are full so adding more makes no difference.
- [Substrate] decreases with time, so rate also decreases with time - therefore the initial rate is the highest rate during a reaction.
- Rate levels off if substrate in excess.
NB = On a volume of x produced by y enzyme/time graph, if line tails off, it is likely because all substrate used up.
Describe competitive enzyme inhibition.
- Inhibitor has similiar structure to the substrate complementary to the enzyme.
- Occupies the enzyme’s active site, competing with the substrate molecules.
- This prevents E-S complexes from being formed.
NB = the relative [substrate]/[inhibitor] determines how much inhibition
i. e. high [inhibitor] = little substrate reaches enzyme active site.
i. e. high [substrate] = will increase chances of substrate reaching enzyme active site and increases rate of inhibited reaction, up to a certain point.
Describe non-competitive inhibition.
- Inhibitors bind elsewhere on the enzyme away from the active site.
- Enzyme shape and therefore active site shape changes.
- Prevents E-S complexes from forming as substrate cannot bind.
- Increase in [substrate] won’t make any significant difference.
How can we see if an enzyme-controlled reaction is being inhibited by competitive or non-competitive inhibition?
Increase the [substrate] and observe rate.
If rate increases, competitive inhibition.
If rate stays virtually constant, non-competitive inhibition.
Describe end-product enzyme inhibition (+).
Enzymes at the start of a metabolic pathway are inhibited more or less by the product of the pathway.
Basically a system of negative feedback - high product concentration - less needed so enzyme A at start of pathway inhibited so less produced and works vice versa.
Usually non-competitive inhibition.
=> Ensures an almost constant [product].
Functions of DNA and RNA - generally.
DNA - holds genetic information, coding for proteins. Long polynucleotide chain.
RNA - transfers genetic information from DNA to the ribosomes. Relatively short polynucleotide chain.
DNA nucleotide structure.
RNA nucleotide structure.
Deoxyribose 5C sugar, bonded to an organic nitrogenous base on C1 and to a phosphate group on C4.
Ribose 5C sugar, bonded to an organic nitrogenous base (T replaced by U) on C1 and to a phosphate group on C4.
Importance of condensation reactions in forming DNA.
Bonds holding nucleotide together are formed by condensation reactions.
Phosphodiester bonds (bonds between individual nucleotides - C3 on sugar and phosphate) formed by condensation reactions.
Complementary base pairing occurs between which nitrogenous bases? How many H-bonds?
Adenine – Thymine. 2 x H-bonds.
Cytosine —Guanine. 3 x H-bonds
DNA is in what form? Why is it a stable molecule?
Long polynucleotide chain coiled into a double helix due to hydrogen bonding between the bases. Antiparallel polynucleotide strands run in opposite directions.
Stable because:
- Phosphodiester backbone protects the more chemically reactive organic bases inside the double helix.
- MANY hydrogen bonds link the organic base pairs, adding more stability. More C—G pairing leads to a more stable DNA molecule, as more H-bonds.
DNA’s structure-function relationship.
- Stable, hereditary structure which rarely mutates.
- 2 separate DNA strands joined by H-bonds so can be separated in DNA replication and protein synthesis.
- Extremely large molecule - holds lots of genetic information.
- Base pairs within the helical cylinder - largely protected by external chemical and physical forces.
- Base pairing leads to DNA being able to replicate and to transfer information as mRNA.