It is a aspartyl protease.
Enzymes act as catalysts.
It indicates that the reaction is non-spontaneous and favors the reactants.
A substrate bound to an enzyme, providing a unique microenvironment for the reaction.
By a factor of 10^9.
It indicates that the reaction rate approaches a maximum as substrate concentration increases.
It undergoes a conformational change that allows catalytic groups to be near the substrate.
Serine forms the covalent enzyme-substrate complex.
It increases the rate of the reaction.
Metal Ion.
It cleaves viral polyproteins into functional proteins necessary for HIV replication.
A metal present in the active site activates the carbonyl, allowing for direct attack of water.
Excess solute will not dissolve and may precipitate out of the solution.
A negative free energy change indicates that a reaction is spontaneous, but it does not guarantee a fast reaction rate.
It stabilizes the positive charge on histidine.
It indicates the ratio of the concentrations of products to reactants at equilibrium.
Chymotrypsin, which forms a covalent acyl-enzyme intermediate during peptide bond hydrolysis.
It provides a pathway for the reaction that is different from the non-catalyzed reaction, often leading to increased specificity and efficiency.
Cofactors assist enzymes in catalyzing reactions, enhancing their activity.
Chymotrypsin is a protease.
Rate constants are inversely related to activation free energy; as activation energy decreases, the rate constant increases.
The rate constant will be low.
It describes the condition where the concentration of the enzyme-substrate complex remains constant over time.
They lower the activation energy required for reactions.
They increase the rate of chemical reactions without being consumed in the process.
It is formed when an enzyme binds to its substrate, facilitating the conversion to product.
A type of catalysis where a temporary covalent bond is formed between the enzyme and the substrate.
It lowers the activation energy, making the reaction proceed more easily.
Nucleophiles attack electrophilic centers in the substrate, forming a covalent intermediate.
Yes, depending on their environment and the reaction conditions.
As substrate concentration increases, the velocity increases until it reaches a maximum velocity (Vmax).
An inorganic ion or a coenzyme required for enzyme activity.
Enzymes are typically named based on the substrate they act upon or the type of reaction they catalyze.
Catalysis by the constituents of water, involving proton donation by hydronium ion (H3O+) or proton acceptance by hydroxyl ion (OH-).
Initial velocity increases and eventually levels off.
It refers to the decrease in disorder or randomness when a substrate binds to an enzyme.
It refers to the point at which a solution can no longer dissolve additional solute.
It acts as the nucleophile that attacks the substrate.
It acts as a general base and acid during the reaction.
Enzymes are specific to their substrates, ensuring that only particular reactions occur.
k1 for the formation of E:S, k2 for the reverse reaction, and k3 for the conversion to product P.
The equilibrium between free enzyme E and substrate S forming the enzyme-substrate complex E:S.
Enzyme catalysts are highly specific to their substrates.
Enzymes can catalyze multiple reactions in a short time, increasing overall efficiency.
An enzyme that is associated with its cofactor.
In the active site.
A process where metal ions facilitate chemical reactions by stabilizing negative charges or participating in redox reactions.
Entropy reduction contributes to the specificity by favoring the formation of a stable complex.
To stabilize the transition state and lower the activation energy of a reaction.
It allows enzymes to selectively bind to specific substrates, enhancing reaction efficiency.
It is formed when an enzyme binds to its substrate, facilitating the conversion to products.
The ionization state of amino acids changes with pH, affecting their catalytic activity.
They laid the foundation for understanding enzyme kinetics.
Enzyme catalysts can significantly increase reaction rates, often by several orders of magnitude.
An organic cofactor required for the action of certain enzymes, often synthesized from a vitamin.
The suffix '-ase' is commonly used for enzymes.
Enzyme catalysis, kinetics, mechanism, and regulation.
A lower activation free energy increases the reaction rate.
Factors include enzyme structure, substrate concentration, and environmental conditions.
Catalytic groups come into proximity with the substrate.
Inhibiting HIV protease prevents the maturation of the virus, thereby stopping its replication.
The active site is crucial for the enzyme's ability to bind to substrates and catalyze the cleavage of peptide bonds.
The reaction rate is not directly related to the free energy change; instead, it is influenced by the activation energy and the presence of catalysts.
It stabilizes the enzyme-substrate complex, facilitating the reaction.
E + S ⇌ E:S → E + P
It is essential for the enzyme's catalytic activity and specificity.
The carbonyl bond breaks, leading to the formation of a tetrahedral intermediate.
Metabolic side effects, such as lipid abnormalities.
A coenzyme or cofactor that is tightly associated with the protein, sometimes covalently.
Enzymes are classified into six main categories based on the type of reaction they catalyze.
They lower the activation energy required for reactions.
Acid/Base.
Covalent.
It helps to understand enzyme mechanisms and the effects of inhibitors on enzyme activity.
It increases the rate of the reaction.
By coordinating with substrates and lowering the activation energy required for the reaction.
It processes viral proteins that are essential for the assembly and maturation of new virions.
Common metal ions include zinc, iron, copper, and magnesium.
By stabilizing the transition state and lowering the activation energy.
It helps enzymes selectively bind to specific substrates.
They bind to the active site of the protease, preventing it from cleaving polyproteins.
Protonation of the tetrahedral intermediate to regenerate the carbonyl group.
Ribozymes, which are catalytic RNA molecules.
Hyperbolic.
Involves the donation or acceptance of a proton by weak acids and bases other than water.
Specific and General.
The binding of the substrate causes a conformational change in the protein.
They include substrate binding, transition state stabilization, and product release.
Enzymes act as catalysts.
Two active site Asp residues facilitate the direct attack of water on the carbonyl group.
It stabilizes the enzyme-substrate complex, facilitating the catalytic process.
By stabilizing the transition state and providing an alternative reaction pathway.
A set of three key amino acids: serine, histidine, and aspartate.
Yes, many enzymes utilize metal ions as cofactors to enhance their catalytic activity.
Amino acids can donate or accept protons, facilitating the reaction.
The side chains can have functional groups that act as acids or bases.
Catalysts lower the activation energy, which can increase the reaction rate without changing the free energy change.
Histidine can easily switch between protonated and deprotonated forms, making it a key player.
Activation energy is the minimum energy required for a reaction to occur, influencing the reaction rate.
Michaelis and Menten.
The binding energy is released when the enzyme-substrate complex forms, contributing to the overall energy change of the reaction.
It signifies that the reaction is spontaneous and favors the formation of products.
They determine the rates of formation and breakdown of the enzyme-substrate complex and the formation of product.
It indicates that the system is at equilibrium, and K = 1.
Enzymes can function effectively at lower temperatures and pressures compared to inorganic catalysts.
An enzyme without its cofactor.
Oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
Lactase, which acts on lactose.
Cysteine serves the catalytic role of forming the covalent enzyme-substrate complex.
It lowers the activation energy, making the reaction more favorable.
The energy required to separate a system into its individual components.
It can limit the availability of substrate for the enzyme, impacting reaction rates.
Saturation occurs at a specific concentration where no more solute can dissolve.
A strong nucleophile, such as an alkoxide or a hydride.
ΔG = -RT ln(K), where R is the gas constant and T is the temperature in Kelvin.
They help reduce viral load and improve immune function in infected individuals.
A biological catalyst that enhances the reaction rate but remains unchanged in the reaction.
DNA polymerase, which synthesizes DNA.
They can undergo oxidation and reduction, allowing them to transfer electrons during the reaction.
Temperature, pH, substrate concentration, and enzyme concentration.
A reaction involving a carbonyl group (C=O) where nucleophiles attack the carbon atom.
To cleave viral polyproteins into functional proteins necessary for HIV replication.
Nucleophilic attack on the carbonyl carbon.
Effective binding increases the likelihood of substrate conversion to product, thus increasing the reaction rate.
Ritonavir, Saquinavir, and Lopinavir.
The region where the substrate binds and must be properly oriented for catalysis to occur.
