If you multiplied enzyme concentration by kcat, think about what you would get. Which one of the following would be suitable units? unitless, because the numerator and denominator would both have the same units O s1 M-1 (s) x (M) O Ms

You are working on an enzyme that obeys standard Michaelis-Menten kinetics. Based on the following reaction expression, what is the Km value for this enzyme? E+SESE + P . . . k₁ = 880.8 M-¹5-1 k.₁ = 42.18 S-1 k₂ = 56.29 S-1

A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction: HAPPY-SAD The researchers begin to characterize the enzyme. The researchers determined the kcat of the enzyme to be 452 s-1. In a separate experiment with [E;) at 1.5 nM and [HAPPY) at 38 µM, the researchers find that Vo is equal to 320 nM s-1. What is the measured Km of happyase* for its substrate HAPPY? Make sure to include units in the answer.

Draw the Michaelis-Menten graph you would predict for the enzyme using 50 nM and 100 nM of enzyme in your assays.

An enzyme contains an active site aspartic acid with a pKa = 5.0, whichacts as a general acid catalyst. On the accompanying template, draw thecurve of enzyme activity (reaction rate) versus pH for the enzyme (assumethat the protein is stably folded between pH 2–12 and that the active siteAsp is the only ionizable residue involved in catalysis). Briefly explain theshape of your curve.

If 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.

A purified protein fraction has a total sample volume of 360 µL.  The sample has a corrected A280 of 0.484, and the blank corrected A280 was 0.052.  (Both values were measured with a path length of 1.00 cm.)  If 5.00 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).

Calculate 1/[S] and 1/V to complete the table. Use this data to draw a Lineweaver-Burke plot, with lines for ‘no inhibitor’ and ‘with inhibitor’. Be sure to label your axes and lines.  What kind of inhibitor is it? Estimate Vmax and Km for the uninhibited reaction.