- Enzyme specificity.
- Cooperative binding, related to its quaternary structure.
- Irreversible denaturation.
- Competitive inhibition.
Category: Macro Mulecule
- The irreversible binding of substrate.
- The dynamic conformational changes that enzymes undergo during catalysis.
- The effect of temperature on enzyme activity.
- The requirement for cofactors.
- Dehydration synthesis.
- Enzymatic hydrolysis or denaturation.
- Polymerization.
- Genetic recombination.
- Placing it in distilled water.
- Exposing it to its optimal pH.
- Heating it far beyond its optimal temperature.
- Increasing substrate concentration.
- Structural.
- Transport.
- Hormonal.
- Immunological.
- Tertiary structure.
- Quaternary structure.
- Primary structure.
- Secondary structure.
- Primary.
- Secondary.
- Tertiary.
- Quaternary.
- Are larger than their substrates.
- Can function at any temperature.
- Provide a specific microenvironment (active site) that facilitates the reaction.
- Are consumed in the reaction.
- Energy storage.
- Structural components, forming the bilayer.
- Acting as enzymes.
- Genetic information storage.
- The highest possible kinetic energy of the molecules without causing denaturation.
- Complete denaturation of the enzyme.
- Lowest possible activation energy.
- Reduced substrate concentration.
- The central alpha-carbon.
- The amino group.
- The carboxyl group.
- The unique R-group (side chain).
- Simple proteins from globular proteins.
- Fibrous proteins from simple proteins.
- Conjugated proteins from simple proteins.
- Derived proteins from conjugated proteins.
- Decreased reaction rate.
- Increased activation energy.
- Increased frequency of enzyme-substrate collisions.
- Decreased enzyme specificity.
- Monosaccharide.
- Nucleotide.
- Amino acid.
- Fatty acid.
- Catalyze a wide range of reactions.
- Bind to and act upon only one or a very limited number of substrates.
- Function at any temperature or pH.
- Be synthesized rapidly by the cell.
- The primary structure is broken.
- The amino acid sequence is altered.
- The protein refolds into a random, non-functional shape that is difficult to reverse.
- The protein gets completely hydrolyzed.
- Structural protein.
- Transport protein.
- Hormonal protein.
- Storage protein.
- They are rapidly consumed outside these ranges.
- Their three-dimensional active site structure is maintained within these ranges, but distorted outside.
- They cannot bind to substrates outside these ranges.
- Their rate of synthesis is highest in these ranges.
