Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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The enzymes are biochemical catalysts that enhances the rate of biological reactions.
Most enzymes are protein in nature although some NA molecules also sow enzymatic activity.
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- How temperature, pH and salt affects the enzyme activity in terms of protein structure (primary, secondary, tertiary, quaternary) and other factors? Please explain briefly.arrow_forwardWhen 10 micrograms of an enzyme with a molecular mass of 80,000 Daultons (grams/mol) is added to a solution containing its substrate at a concentration 100 times the Km, it catalyzes the conversion of 65 micromoles of substrate into product in 3 minutes. What is the enzyme's turnover number (in units of min-1)?arrow_forwardHow can you find Kcat if you are only given Vmax, Km and [E] ? I tried using Kcat=Vmax/[E] but that didn't work. How do you know if [E] is the same as [E]total, and if it isn't how do you find it from this information: The Vmax for a particular enzyme is 10 nmols/L/s. The Km for its substrate is 5 microM. If the enzyme concentration is 10 nM, what is the kcat? a.80 nmoles/L/s b.8000 nmoles/L/s c.2 nmoles/L/s d.50 nmoles/L/sarrow_forward
- For a Michaelis-Menten reaction, k₁=5 x 107/M-s, k-1-2 x 104/s, and k2=4 x 10²/s. Calculate the Ks and KM for this reaction. Does substrate binding achieve equilibrium or steady state?arrow_forward82.16arrow_forwardWrite the balanced reaction catalyzed by phophoenolpyruvate carboxylase (P PC). Remember to add any cofactors, and to draw the structure formulas (a line-bond representation is fine) for the main substrate and product of the reaction.arrow_forward
- Lisa decides to obtain values for the Km and Vmax of an enzyme that was isolated from liver cells.. Using the Michaelis Menten plot. In what kind of measurements are needed and what would be needed to plot on a graph to estimate Km and Vmax?arrow_forwardIf you want to determine the KM for lactate, what protocol do you set up? Discuss the significance of the following kinetic parameters that are used to characterize enzyme activity: KM, Vmax, kcat, and kcat / KM.arrow_forwarda) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and D-DOPA? Show any relevant analyses or calculatins you did to determine these values. ( HINT a graph might be helpful here! ) b) Based on your answer to part a, briefly describe how the kinetics of the enzyme differs for the two substrates. Which Substrate has better binding affinity to the enzymearrow_forward
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