In the hydrolysis of p-nitrophenylacetate by chymotrypsin all of the following are correct (mark all the correct answers): Group of answer choices the active site contains a serine residue, an unprotonated histidine, and an unprotonated aspartate residue at pH 7.0 prior to binding the substrate. attack of a water molecule on the acyl-enzyme intermediate yields the second product. the first product is acetic acid. an acetyl-enzyme intermediate forms during the mechanism.

-- the active site contains a serine residue, an unprotonated histidine, and an unprotonated aspartate residue at pH 7.0 prior to binding the substrate.

--  attack of a water molecule on the acyl-enzyme intermediate yields the second product.

-- an acetyl-enzyme intermediate forms during the mechanism.

Explanation:

p-Nitrophenyl acetate is a chemical compound and is used as a substrate in the assays for esterase as well as lipase activity.

Doing hydrolysis of the p-nitrophenyl acetate releases a p- nitrophenol, and its absorbance can be monitored at about 405 nm.

In doing hydrolysis of the p-nitrophenyl acetate by a chymotrypsin, the following holds true :

the dissociation of nickel hydroxide is follows:

the concentration of hydroxide ion is

the equilibrium constant value of nickel hydroxide is = 6.1 * 10^-^1^6 and thus equilibrium equation can be written as:

thus, concentration of ni is 0.23 * 10^-^4 mol /l