Q. The phenomenon which involves formation of an additional covalent intermediate in a reaction that helps to reduce the energy of later transition states is referred to as ___________

View solution

Q. Chymotrypsin: Nucleophilic catalysis:: Carboxypeptidase A: __________

View solution

Q. A type of catalysis which involves covalent intermediate transition state formation between the cationic electrophilic group in the enzyme and the electron rich portion of the substrate is referred to as ____________

View solution

Q. _____________ involves donation of electrons from nucleophilic active site residues to a substrate forming a covalent adduct transition state intermediate.

View solution

Q. Which of these is not required for electrophilic catalysis?

View solution

Q. Which of the following assumption was not made in rapid equilibrium model?

View solution

Q. Which of these is referred to as Kcat?

View solution

Q. What does the following equation represent?

\(\frac{1}{V_0} = \frac{K_m}{V_{max}} \frac{1}{[S]}+\frac{1}{V_{max}}\)

View solution

Q. Which of the following is based on rearrangement of Lineweaver Burk plot equation by multiplication of [S₀] factor?

View solution

Q. Miachelis Menten model is also referred to as “rapid equilibrium model”.

View solution

Q. ___________ is defined as the enzyme’s binding efficiency with its appropriate substrate through optimized multiple non-covalent interactions.

View solution

Q. 4*10⁷: Catalase :: 25: ___________

View solution

Q. What is the ratio of V₀/Vₘₐₓ when [S] = 10Kₘ?

View solution

Q. What does the equation \(V_0=\frac{V_{max} [S]}{K_m+[S]}\) represent?

View solution

Q. Which of the following is termed as catalytic efficiency?

View solution

Q. Which of the following equation is Eadie-Hofstee plot equation?

View solution

Q. The equation which is based on reciprocal form of Miachelis Menten equation at constant [Et] level is referred to as ______________

View solution

Q. ______________ is defined as an enzyme molecule’s efficiency to convert maximum substrate molecules into product per unit time.

View solution

Q. A low Kₘ value points out a low affinity of an enzyme towards its substrate.

View solution

Q. Given an enzyme with Kₘ of 0.25mM, at what substrate concentration will the velocity of the enzyme reach 1/2 of the Vₘₐₓ? (Vₘₐₓ = 100 mmol/s)

View solution