Biochemistry Exam 2 | Biochemistry Module Exam 2 | Biochemistry ACTUAL
Exam 2 COMPLETE QUESTIONS WITH 100% RATED CORRECT
ANSWERS 2025 LATEST UPDATED GRADED A+| GET IT CORRECT!!
Which of the following statements BEST describes the Michaelis-Menton constant KM? -
(answer)it is numerically equal to the substrate concentration required to reach half maximal
velocity for an enzyme-catalyzed reaction
Vmax - (answer)rate of a reaction when enzyme is saturated with substrate
Kcat - (answer)number of susbtrate molecules turned over by enzyme
Kcat/Km - (answer)enzyme efficiency
Km - (answer)a substrate concentration at 0.5 Vmax
A mutation causing an amino acid change in an enzyme that affects the turnover number kcat
will always affect the KM as well. - (answer)false!
A Lineweaver-Burk plot can be used to determine KM using initial-rate data for an enzyme-
catalyzed reaction. - (answer)true
competitive inhibitor - (answer)has a structure that is so similar to the substrate that it can bond
to the enzyme just like the substrate
noncompetitive inhibitor - (answer)binds to a site on the enzyme that is not the active site. When
this occurs, the shape of the enzyme is distorted
irreversible inhibitor - (answer)forms a covalent bond with an amino acid side group within the
active site, which prevents the substrate from entering the active site or prevents catalytic activity
Exam 2 COMPLETE QUESTIONS WITH 100% RATED CORRECT
ANSWERS 2025 LATEST UPDATED GRADED A+| GET IT CORRECT!!
Which of the following statements BEST describes the Michaelis-Menton constant KM? -
(answer)it is numerically equal to the substrate concentration required to reach half maximal
velocity for an enzyme-catalyzed reaction
Vmax - (answer)rate of a reaction when enzyme is saturated with substrate
Kcat - (answer)number of susbtrate molecules turned over by enzyme
Kcat/Km - (answer)enzyme efficiency
Km - (answer)a substrate concentration at 0.5 Vmax
A mutation causing an amino acid change in an enzyme that affects the turnover number kcat
will always affect the KM as well. - (answer)false!
A Lineweaver-Burk plot can be used to determine KM using initial-rate data for an enzyme-
catalyzed reaction. - (answer)true
competitive inhibitor - (answer)has a structure that is so similar to the substrate that it can bond
to the enzyme just like the substrate
noncompetitive inhibitor - (answer)binds to a site on the enzyme that is not the active site. When
this occurs, the shape of the enzyme is distorted
irreversible inhibitor - (answer)forms a covalent bond with an amino acid side group within the
active site, which prevents the substrate from entering the active site or prevents catalytic activity
