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Enzyme Kinetics

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Total cards: 10•Content version: v4•Public deck•Updated: 8/1/2026

Card preview (10)

#1
Front (Question)

What is the shape of the graph plotted of reaction rate against substrate concentration? How do we estimate Km using this?

Back (Answer)

Hyperbolic graph and then levels out Km is the substate concentration at half the Vmax

#2
Front (Question)

What is the Michealis - Menton equation regulated by? What rule must there be for it to work?

Back (Answer)

Kinetic constants K-1»>K2

#3
Front (Question)

What are 3 assumptions we must have?

Back (Answer)

• concentration of substate is much larger than that of the enzyme so the amount of substrate bound by an enzyme is always small • Enzyme substate concentration does not change with time • Initial velocities must be used

#4
Front (Question)

What is the equation for MM?

Back (Answer)

Initial velocity = Vmax[S] / Km + [S]

#5
Front (Question)

When the MM is plotted, what shape is it and what kinetic value does it tend towards?

Back (Answer)

Hyperbolic and it tends towards Vmax

#6
Front (Question)

The lower the Km, the — the affinity?

Back (Answer)

Higher

#7
Front (Question)

What does the Kcat mean?

Back (Answer)

The turnover number of substrates to products over time

#8
Front (Question)

What do competitive inhibitors alter and not alter?

Back (Answer)

Alter the Km value but not the Vmax

#9
Front (Question)

What do non-competitive inhibitors alter?

Back (Answer)

Vmax

#10
Front (Question)

What 2 clinical examples can this help?

Back (Answer)

Control of angiotensin production Treatment of heart failure