Macromolecules 2 Flashcards
What is an enzyme? What do they do and what are they made of?
Biological macromolecule that catalyzes biochemical reactions. They are large protein molecules so they are composed of long amino acid chains folded into particular three dimensional shapes. Can have primary, secondary, tertiary or quaternary structures.
Would enzymes be used up in a reaction?
Never used up in a reaction as they are catalysts.
What is a turnover number?
The number of substrate molecules turned into product/catalytic site/unit time.
What is the turnover number of catalase?
40x10^7/ second
What is the turnover number for amylase?
18000/second`
What are the three types of enzyme specificity?
Absolute, Group and linkage specificities
What is absolute specificity?
They enzyme only catalyzes one reaction
What is Group specificity?
The enzyme only acts on molecules that have specific functional groups (amino groups, phosphate groups and methyl groups)
What is linkage specificity?
The enzyme acts on a particular type of chemical bond regardless of the rest of the molecular structure
How is enzyme efficiency measured?
By the turnover number
Characteristics of enzymes? (7)
- Organic molecules
- Shape is complementary to the shape of their respective substrate
- Turn substrates into products
- Never used up
- do not alter the outcome, only the speed of reaction
- End in -ase
- Prefix is related to its substrate or function (lactase catalyzes lactose)
What are enzymes that catalyze hydrolysis reactions called?
Hydrolases
What is activation energy?
Energy required to initiate a chemical reaction
What is a catalyst?
Substance that speeds up the rate of a reaction
What is a substrate?
A reactant that interacts with the enzyme
What is an enzyme-substrate complex?
Combined structure of an enzyme with a substrate bound to the active site
What is the active site?
The site on an enzyme where a substrate binds
An active site may… (4)
- Contain amino acid R groups that stretch or bend bonds in a substrate to weaken them
- Bring two substrates together in the correct position to get them to bond
- Transfer electrons to and from the substrate to destabilize it and cause it to react
- add or remove electrons from the substrate to destabilize it and cause it to react
Factors that affect enzyme activity include:
Temperature and pH
Enzyme activity increases as substrate concentration ____________
increases
What is an inhibitor?
A molecule that bonds to the allosteric site or active site of an enzyme
What is competitive inhibition?
The inhibitor interacts with the active site of the enzyme, so the substrate and the inhibitor must compete for the active site. It prevents the reaction from happening
What is non-competitive inhibition/allosteric inhibition?
The inhibitor interacts with the allosteric site of the enzyme. The reaction continues normally.
What is the allosteric site?
A site on the enzyme that is not the active site. Here, other molecules can interact with and regulate its activity
What is allosteric regulation?
Regulation of enzyme activity by activators and inhibitors binding to the allosteric parts of an enzyme
What is an activator?
A molecule that binds to the allosteric site of an enzyme and keeps it active or increases enzyme activity
The cell membrane is made up of a phospholipid bilayer and _____________
a mosaic of proteins
True or false, the phospholipids are in fixed place and do not move
False, they move freely because of weak intermolecular forces, which means they can quickly repair any ruptures
What are the three factors that affect the fluidity of the cell membrane?
Temperature, the presence of double bonds, the length of the fatty acid tail
How is the presence of double bonds significant to the fluidity of the membrane?
The more double bonds, the more kinks in the tail and the weaker the london forces.
How is the length of the fatty acid tails significant to the fluidity of the membrane?
Longer tails have more intermolecular interactions and therefore stronger london forces