Enzyme series · lab

Enzyme Lab: watch the inhibitor bind.

A live Michaelis–Menten enzyme. Add substrate and its active sites fill. Add an inhibitor and K_m and V_max move: on the curve, on the Lineweaver–Burk plot, and on the enzymes themselves.

substrateinhibitorproduct Substrate in 4 of 8 active sites

[S]: 2.0mM= K_m
v: 50µM/s½ V_max
K_m: 2.0mM[S] at ½ V_max
V_max: 100µM/sall sites full

Substrate [S]2.0mM

Inhibitor

Nonethe enzyme alone Competitiveactive site, unbound E UncompetitiveES only Noncompetitivesecond site, E or ES Mixedsecond site, unequal

Pick one. You predict what it does before it binds.

Practice it in the course

Watch the Enzyme series78 million years in 18 ms, then the 50× glucose gap between brain and liver Red Pen Prep homeThe course, the trap diagnostic and the other labs

Now one question on it

Same idea, from the course.

From the courseBio/Biochem · D001 Q3

An enzyme that follows Michaelis–Menten kinetics gave these initial rates (v0): 20, 33, 50, 67, 80 µM/s at substrate concentrations of 0.5, 1, 2, 4, 8 mM. Which value is closest to the enzyme’s Km?

Pick one. The red pen does the rest.

This is 1 of 3,122 questions in the Pass, all corrected like this one.

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