Enzyme Basics and Specificity

False (B)

Temperature, pH, enzyme concentration, or substrate concentration

<p>line</p> Signup and view all the answers

<p>To speed up chemical reactions without being consumed (A)</p> Signup and view all the answers

<p>False (B)</p> Signup and view all the answers

<p>Using a gas cylinder to collect oxygen (C)</p> Signup and view all the answers

<p>It is where the substrate binds.</p> Signup and view all the answers

<p>Increasing temperature = Increases rate up to a point Decreasing pH = Can denature the enzyme Increasing substrate concentration = Increases rate until saturation Increasing enzyme concentration = Accelerates the reaction rate</p> Signup and view all the answers

<p>Predictions can be made beyond the range of existing data points.</p> Signup and view all the answers

<p>globular</p> Signup and view all the answers

<p>Intracellular enzymes = Function inside the cell Extracellular enzymes = Secreted by cells to act outside Biological catalyst = Substance that speeds up reactions Metabolic pathways = Series of chemical reactions controlled by enzymes</p> Signup and view all the answers

<p>False (B)</p> Signup and view all the answers

<p>Enzymes are essential for nearly every metabolic reaction in living organisms. (A)</p> Signup and view all the answers

<p>True (A)</p> Signup and view all the answers

<p>Digestive enzymes in the gut.</p> Signup and view all the answers

<p>Temperature (A)</p> Signup and view all the answers

<p>False (B)</p> Signup and view all the answers

<p>Units</p> Signup and view all the answers

<p>smooth</p> Signup and view all the answers

<p>Plot data points accurately = Ensure reliability of the graph Choose appropriate scales = Data fits within the graph area Label axes = Provide information about variables Draw a line of best-fit = Identify trends in the data</p> Signup and view all the answers

<p>When comparing rates at different temperatures (A)</p> Signup and view all the answers

<p>False (B)</p> Signup and view all the answers

<p>The reaction cannot occur.</p> Signup and view all the answers

<p>They denature. (A)</p> Signup and view all the answers

<p>False (B)</p> Signup and view all the answers

<p>pH 2</p> Signup and view all the answers

<p>active site</p> Signup and view all the answers

<p>Optimum pH = pH at which an enzyme operates best Denaturation = Loss of enzyme structure and function Active site = Region where substrate binds to enzyme Hydrogen bonds = Types of bonds that help maintain enzyme structure</p> Signup and view all the answers

<p>They can break ionic and hydrogen bonds in the enzyme. (C)</p> Signup and view all the answers

<p>False (B)</p> Signup and view all the answers

<p>OH- ions</p> Signup and view all the answers

<p>They compete with the substrate for the active site. (B)</p> Signup and view all the answers

<p>False (B)</p> Signup and view all the answers

<p>It reduces the rate of reaction and can stop it completely.</p> Signup and view all the answers

<p>non-competitive</p> Signup and view all the answers

<p>It remains the same at maximal rates. (D)</p> Signup and view all the answers

<p>Competitive Inhibitor = Initial rate lowered but maximal rate unchanged Non-competitive Inhibitor = Both initial and maximal rates lowered</p> Signup and view all the answers

<p>substrate</p> Signup and view all the answers

<p>To slow down or stop enzyme activity.</p> Signup and view all the answers

<p>The active site and substrate fit together perfectly. (A)</p> Signup and view all the answers

<p>False (B)</p> Signup and view all the answers

<p>X-ray diffraction</p> Signup and view all the answers

<p>larger</p> Signup and view all the answers

<p>Lock and Key Model = Active site shape is a perfect fit for the substrate Induced Fit Model = Active site changes shape to fit the substrate Rigid Model = Suggests that proteins do not change shape Flexible Model = Allow for movements in enzyme structure</p> Signup and view all the answers

<p>It doesn't account for the dynamic nature of enzyme structure. (A)</p> Signup and view all the answers

<p>True (A)</p> Signup and view all the answers

<p>The active site changes shape.</p> Signup and view all the answers

Experiments to find out how changing a factor affects how quickly an enzyme-controlled reaction happens.

The factor you change in an experiment to see its effect on the reaction rate.

The factor that changes in response to the independent variable; the thing you measure.

A graph used to show how the reaction rate changes.

A line drawn on a graph to show the overall trend of the data.

Predicting a value between existing data points on a graph.

Estimating a value beyond the range of existing data points.

Amount of enzyme present in a reaction

A biological catalyst that speeds up chemical reactions without being consumed.

Enzymes have a specific shape (active site) that only fits certain substrates.

The part of an enzyme where the substrate binds, crucial for enzyme function.

An enzyme that works inside the cell.

An enzyme that works outside the cell.

A protein with a 3D spherical shape, many enzymes are this type.

A substance that speeds up a chemical reaction without being consumed.

A series of chemical reactions controlled by enzymes to achieve a specific result or target

A graph showing the results of an enzyme experiment, where the independent variable (e.g., substrate concentration) affects the rate of reaction.

A graph that displays data from various conditions (e.g., different temperatures) on a single graph.

The rate of reaction at the beginning of an experiment (determined by the initial gradient of a graph).

The amount of product created in an experiment, often plotted on the y-axis of an enzyme experiment graph instead of reaction rate.

Scales on the axes of a graph that effectively show all data points.

Clearly labeling the axes of a graph with the variables and their units (e.g., temperature in °C).

A model proposing that the active site of an enzyme has a rigid shape perfectly complementary to the substrate, like a lock and key.

A more refined model that suggests the active site of an enzyme adapts its shape to fit the substrate upon binding, like a glove around a hand.

The Lock & Key model proposes a rigid shape for the active site, while the Induced Fit model suggests the active site can change its shape to accommodate the substrate.

X-ray diffraction allows scientists to visualize molecules in 3D, demonstrating the enzyme's shape change before and after the substrate binds.

The specific pH value at which an enzyme functions most efficiently.

The process where an enzyme's structure is permanently altered, losing its functionality.

The active site is where the substrate binds and the chemical reaction occurs, enabling enzymes to facilitate specific reactions.

Enzymes are not rigid structures: they display movement in response to environmental changes, particularly when interacting with substrates.

Extreme pH levels can disrupt the hydrogen and ionic bonds holding the enzyme's structure together, leading to denaturation.

Enzymes act as biological catalysts, speeding up chemical reactions in living organisms, enabling vital biological processes.

Pepsin, an enzyme in the stomach, has an optimum pH of 2 due to the acidic environment created by hydrochloric acid.

The best environment for an enzyme is determined by its specific optimum pH, reflecting where it naturally functions.

Each enzyme has a specific shape that only fits certain substrates, allowing for precise control of biochemical reactions.

When pH is too high or too low, the enzyme's active site is distorted, hindering its ability to bind to the substrate.

Excess H+ ions (acidic) or OH- ions (basic) disrupt the enzyme's structure by affecting the bonds holding it together.

At extreme pH, the enzyme's structure is completely altered, rendering it incapable of catalyzing any reactions.

Molecules that resemble the substrate and compete for the active site of an enzyme, slowing down or stopping the reaction.

Molecules that bind to a different site on the enzyme, changing the active site's shape and preventing substrate binding.

Inhibitors slow down or stop enzyme-catalyzed reactions by reducing the formation of enzyme-substrate complexes.

Increasing inhibitor concentration leads to a slower reaction rate and eventual complete stoppage of the reaction.

Increasing substrate concentration can overcome the effects of competitive inhibitors by outcompeting them for the active site.

Increasing substrate concentration does not restore the reaction rate in the presence of non-competitive inhibitors, as the active site's shape remains altered.

Competitive inhibitors decrease the initial reaction rate but do not affect the maximal rate. Non-competitive inhibitors decrease both the initial and maximal reaction rates.

Investigate how increasing substrate concentration affects the reaction rate. If the rate increases, it is a competitive inhibitor. If the rate remains low, it is a non-competitive inhibitor.