Enzymes are biological catalysts that speed up chemical reactions in living organisms without being consumed in the process.
Enzymes are proteins that are consumed during a chemical reaction.
Enzymes are lipids that store energy within cells.
Enzymes are vitamins necessary for bodily functions.
Enzymes speed up metabolic processes and chemical reactions within cells, aiding in digestion, respiration, and many other bodily functions.
Enzymes provide structural support to human tissues.
Enzymes transport oxygen throughout the body.
Enzymes serve as the main energy source for cells.
An active site is the specific region on an enzyme where the substrate molecules bind and undergo a chemical reaction.
An active site is the receptor site on a cell membrane.
An active site is where enzymes are synthesized in the cell.
An active site is a stable storage area for enzymes inside cells.
The substrate is the substance upon which an enzyme acts during a chemical reaction.
The substrate is the enzyme that catalyzes a chemical reaction.
The substrate is the energy molecule that powers enzyme function.
The substrate is the by-product of an enzymatic reaction.
Enzymes lower activation energy by binding to the substrate and stabilizing the transition state, making it easier for the reaction to occur.
Enzymes lower activation energy by consuming part of the substrate.
Enzymes lower activation energy by increasing the temperature of the environment.
Enzymes lower activation energy by decreasing the concentration of reactants.
Enzymes increase the rate of a chemical reaction by lowering the activation energy needed for the reaction to proceed.
Enzymes decrease the rate of a chemical reaction by consuming substrates.
Enzymes do not affect the rate of a chemical reaction.
Enzymes reverse the direction of a chemical reaction.
Yes, enzymes can be reused multiple times because they are not consumed by the reaction they catalyze.
No, enzymes can only be used once before being destroyed.
Yes, but only if they are regenerated through additional chemical steps.
No, enzymes are permanently altered by each reaction they catalyze.
Enzyme specificity is the concept that each enzyme catalyzes only one specific type or group of closely related reactions.
Enzyme specificity means all enzymes act on all proteins.
Enzyme specificity varies depending on the amount of substrate.
Enzyme specificity indicates the ability of enzymes to alter their structure during reaction.
As temperature increases, enzyme activity generally increases until the enzyme is denatured by excessive heat. Optimal temperature varies for different enzymes.
Temperature has no effect on enzyme activity.
High temperatures permanently enhance enzyme activity.
Low temperatures inhibit enzyme specificity.
Enzymes have an optimal pH range in which they function best. Deviations from this range can reduce enzyme activity or denature the enzyme.
Enzymes remain unaffected by changes in pH.
Only acidic environments inhibit enzyme activity.
Enzyme activity peaks at pH 7 for all enzymes.
An enzyme-cofactor is a non-protein chemical compound that is required for the enzyme's activity as a catalyst.
An enzyme-cofactor is a protein needed for substrate binding.
An enzyme-cofactor is a genetic material that codes for enzymes.
An enzyme-cofactor is a lipid molecule that stabilizes enzymes.
Enzyme inhibition is the process in which a molecule binds to an enzyme and decreases its activity.
Enzyme inhibition is the acceleration of enzyme activity in high concentrations.
Enzyme inhibition results in the production of more enzymes.
Enzyme inhibition is the process of synthesizing enzymes in low quantity.
Competitive inhibitors are substances that bind to the active site of an enzyme, preventing the substrate from binding and reducing enzyme activity.
Competitive inhibitors bind to substrates instead of enzymes.
Competitive inhibitors enhance the speed of enzyme reactions.
Competitive inhibitors aid enzymes by providing structural support.
Non-competitive inhibitors bind to an enzyme at a site other than the active site, altering the enzyme's shape and function, which reduces its activity.
Non-competitive inhibitors only affect the substrate's structure.
Non-competitive inhibitors increase enzyme activity by enhancing substrate binding.
Non-competitive inhibitors deactivate enzymes permanently.
Enzymes are important in biotechnology for their ability to catalyze specific reactions, which can be used in processes like fermentation, waste management, and pharmaceuticals.
Enzymes are rarely used in biotechnology due to their instability.
Enzymes in biotechnology are used to store genetic information.
Enzymes provide structural components for bioengineering projects.