KIVO Med
Allosteric enzymes
The structural, kinetic, and regulatory principles that let certain enzymes control a metabolic pathway.
- 20 explained questions
- 19 flashcards
- 84 estimated course minutes
Updated
What you will learn
- Distinguish active and allosteric sites, protomers, and T or R states.
- Read a sigmoid kinetic profile and explain cooperativity.
- Compare concerted and sequential models and distinguish homotropic from heterotropic effects.
Course outline
A control point within a metabolic pathway
Locate the role of an allosteric enzyme in flux control before detailing its mechanisms.
9 min
Sites, protomers, and T/R states
Understand how quaternary architecture makes an allosteric transition possible.
18 min
Cooperative kinetics
Read a sigmoid curve, the Hill equation, and the link between cooperativity and the T–R transition.
22 min
Two models for cooperativity
Compare concerted and sequential transitions of enzyme subunits.
16 min
Homotropic and heterotropic effects
Identify the binding molecule, the site involved, and the consequence for substrate affinity.
19 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.
Enzyme kinetics
Relate enzymatic reaction rate to concentrations, kinetic constants, and measurement methods.
Modulation of enzymatic activity
Understand how pH, temperature, ions, radiation, inhibitors, and activators modify an enzymatic reaction.