KIVO Med
Enzyme kinetics
Relate enzymatic reaction rate to concentrations, kinetic constants, and measurement methods.
- 15 explained questions
- 15 flashcards
- 90 estimated course minutes
Updated
What you will learn
- Define an initial rate and the conditions used to measure it.
- Derive and interpret the Michaelis–Menten equation.
- Distinguish Vmax, Km, kcat, and the specificity constant.
- Read Michaelis–Menten, Lineweaver–Burk, and Eadie–Hofstee representations.
- Calculate enzymatic activity and identify the main two-substrate mechanisms.
Course outline
From chemical transformation to measurable speed
Understand what enzymatic kinetics measures and why analysis begins at the start of the reaction.
12 min
Measuring initial speed and recognising saturation
Define $V_i$, distinguish orders 1 and 0, and relate enzyme concentration to the speed plateau.
15 min
Building the Michaelis–Menten model
Move from the enzyme–substrate mechanism to the relation between initial speed, substrate, $K_m$, and $V_{max}$.
21 min
Interpreting constants and measuring enzyme activity
Use $V_{max}$, $K_m$, $k_{cat}$, $k_{cat}/K_m$, and absorbance to characterise an enzyme.
25 min
Distinguishing two-substrate mechanisms
Recognise random and ordered sequential mechanisms, and distinguish them from ping-pong catalysis.
17 min
Study and practise with KIVO Med
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Educational resources for medical studies; they do not replace your faculty’s teaching or medical advice.
In the same subject
Enzymology: structure and mechanisms of action
Understand what makes an enzyme catalytically active, specific, regulatable and identifiable through its nomenclature.
Modulation of enzymatic activity
Understand how pH, temperature, ions, radiation, inhibitors, and activators modify an enzymatic reaction.
Allosteric enzymes
The structural, kinetic, and regulatory principles that let certain enzymes control a metabolic pathway.