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Well using less pepsin means you have less of the enzyme. Now if you keep the substrate / enzyme ratio constant there won't be anything changing. If you however decrease the pepsin amount, there will be less active sites for the same amount of substrate to bind. ---> slower reaction
What else can I help you with?
How can one determine both the KM and Vmax values for a given enzyme-catalyzed reaction?
To determine the KM and Vmax values for an enzyme-catalyzed reaction, one can perform a series of experiments measuring the initial reaction rate at different substrate concentrations. By plotting the data using the Michaelis-Menten equation, the KM value can be determined as the substrate concentration at half of Vmax. Vmax is the maximum reaction rate achieved when all enzyme active sites are saturated with substrate.
What reaction would represent dephosphorylation?
Dephosphorylation is the process of removing a phosphate group from a molecule. For example, the reaction catalyzed by a phosphatase enzyme can dephosphorylate a substrate by removing the phosphate group from it, typically using water as a reactant. This reaction decreases the phosphorylation state of the molecule, impacting its biological activity and signaling.
What is the hydrolysis of serylglycine?
The hydrolysis of serylglycine involves breaking the peptide bond between the amino acid serine and glycine using water molecules. This reaction is catalyzed by enzymes known as peptidases, resulting in the formation of serine and glycine as separate amino acids.
What is enzyme coupling?
Some enzyme-catalyzed reactions do not involve changes in substrates, products, or cofactors that have easily observable properties (e.g. changes in light absorbance, etc) for the measure of reaction kinetics. In such cases, additional enzymes may be included in the reaction mixture that catalyze a reaction using the product of the first enzymatic reaction as a substrate, metabolizing it to a compound that has more easily measurable properties. If this second reaction is much faster than the first, the kinetics of the overall path approximate the kinetics of the slower reaction alone. This technique can also be used to move spectral peaks of a substrate farther away from those of interfering species, such as peaks normally observed around 280 nm for proteins (due mostly to absorbances oftryptophan, tyrosine and cysteine residues) .
A reaction can be described using a word?
A reaction that can be described using a word
A chemical equation for the preaparation of 4-methylcyclohexene from 4-methylcyclohexanol?
4-methylcyclohexanol can be dehydrated to form 4-methylcyclohexene using concentrated sulfuric acid as a catalyst. The reaction can be represented by the following chemical equation: 4-methylcyclohexanol → 4-methylcyclohexene + H2O
Protein digestion by pepsin what is the significance of using 37 degree Celsius for the incubation?
That's the average human body temperature.
When using a step down transformer is amperage affected?
Yes, when using a step down transformer the amperage is affected.
To determine the rate of a reaction using the rate law?
The rate of a reaction is calculated using the concentrations of reactants.
What determines the rate of a reaction using the rate law?
The rate of a reaction is calculated using the concentrations of reactants.
Who is most affected by marijuana?
The person using it.
How do you stop a or slow a chemical reaction?
by using an inhibitor or poisoning the chemical reaction
