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Bioc 3021 Exam 2 Questions and Answers 100% Solved | Latest Update

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Bioc 3021 Exam 2 Questions and Answers 100% Solved | Latest Update Michaelis- Menten Equation - The velocity of an enzyme reaction (V) is equal to the maximum reaction velocity (Vmax) times the substrate concentration (S) divided by substrate concentration plus the Michaelis constant ( Km) in...

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  • December 7, 2024
  • 19
  • 2024/2025
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  • Questions & answers
  • Bioc 3021
  • Bioc 3021
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Bioc 3021 Exam 2 Questions and

Answers 100% Solved | Latest Update


Michaelis- Menten Equation - ✔✔The velocity of an enzyme reaction (V) is

equal to the maximum reaction velocity (Vmax) times the substrate

concentration (S) divided by substrate concentration plus the Michaelis

constant ( Km)

increases - ✔✔Rate of product formation ____________ as the initial

substrate concentration is raised.

Velocity - ✔✔How rapidly product is being formed by the reaction

Vmax - ✔✔Fastest reaction rate possible

S - ✔✔Substrate concentration

Km - ✔✔Michaelis constant ( dimensions of concentration)

Linear Km reduces to V= K x S (equation for a straight line) - ✔✔At low S

values the plot is _______

Curved

Need to use the entire Michaelis- Menten equation


1
©JOSHCLAY 2024/2025. YEAR PUBLISHED 2024.

,+ 1/2 Vmax - ✔✔At intermediate S values the plot is _____________

v= Vmax - ✔✔At high S values the plot is ________

Active sites available - ✔✔The rate of the reaction is limited by the number

of _________________.

Efficient - ✔✔Enzymes having a LOW Km are _______ at low substrate

concentrations

Inefficient - ✔✔Enzymes having a HIGH Km are ________ at low substrate

concentrations

Turnover number - ✔✔The number of molecules of substate that can be

converted per second per molecule of enzyme of a specific enzyme

Line Weaver Burk Plot - ✔✔Alternate plot used for plotting kinetic data can

be derived by inverting the Michaelis- Menten equation you plot 1/v + 1/s,

now you get a straight line

1/ Vmax - ✔✔1/ V intercept =

-1/ Km - ✔✔1/S intercept =

Km/ Vmax - ✔✔Slope of line =

Inhibitors - ✔✔__________ interfere with enzymatic activity.

Reversible - ✔✔


2
©JOSHCLAY 2024/2025. YEAR PUBLISHED 2024.

, Irreversible - ✔✔Covalently modify an enzyme and inhibition cannot be

revered

Competitive - ✔✔Bind to the active site of the enzyme and compete with

the substrate



At high substrate levels the effect of the inhibitor can be overcome, at high

inhibitory concentrations it is very unlikely the substrate will bind



The ratio of [inhibitor] to [substrate] determines the degree of activity

Non- Competitive - ✔✔Bind somewhere else on the enzyme (not the active

site) and inhibit by causing some change transmitted through the enzyme

to the active site



Raising the substrate concentration does not effect the degree of activity

slow - ✔✔Competitive inhibitors have _______ reaction rates

Competitive inhibitor can not bind - ✔✔At high [S] there is so much S that

_______ ____

The Vmax stays the same and the Km increases - ✔✔If a competitive

inhibitor is added to an enzyme reaction then:

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©JOSHCLAY 2024/2025. YEAR PUBLISHED 2024.

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