N = 3
O = -2
1(3) +2(-2)= -1
Answer:
(2) Half of the active sites are occupied by substrate.
Explanation:
The Michaelis–Menten equation is the rate equation for a one-substrate enzyme-catalyzed reaction. It is an expression of the relationship between the initial velocity V₀ of an enzymatic reaction, the maximum velocity Vmax, and substrate concentration [S] which are all related through the Michaelis constant, Km.
Mathematically, the Michaelis–Menten equation is given as:
V₀ = Vmax[S]/Km + [S]
A special relationship exists between the Michaelis constant and substrate concentration when the enzyme is operating at half its maximum velocity, i.e. at V₀ = Vmax/2
substituting, Vmax/2 = V₀ in the Michaelis–Menten equation
Vmax/2 = Vmax[S]/Km + [S]
dividing through with Vmax
1/2 = [S]/Km + [S]
2[S] = Km + [S]
2[S] - [S] = Km
[S] = Km
Therefore, when the enzyme is operating at half its maximum velocity, i.e. when half of the active sites are occupied by substrate, [S] = Km
Answer:
The gallbladder is a pear-shaped, hollow structure located under the liver and on the right side of the abdomen. Its primary function is to store and concentrate bile, a yellow-brown digestive enzyme produced by the liver. The gallbladder is part of the biliary tract