KIVO Med
Enzymology: structure and mechanisms of action
Understand what makes an enzyme catalytically active, specific, regulatable and identifiable through its nomenclature.
- 15 explained questions
- 15 flashcards
- 86 estimated course minutes
Updated
What you will learn
- Define enzyme, substrate, product, ligand, cofactor, apoenzyme and holoenzyme.
- Relate protein organisation and the active site to specificity and catalysis.
- Distinguish free coenzymes from prosthetic groups and identify the properties of isoenzymes.
- Read an EC designation and recognise the six enzyme classes studied.
Course outline
A map of cellular catalysis
Connect reaction acceleration, enzyme structure, and the role of enzymes in metabolic balance.
10 min
Participants in an enzymatic reaction
Distinguish substrate, product, ligand, cofactor, apoenzyme, and holoenzyme.
16 min
Protein architecture and the active site
Relate the levels of enzyme organisation to the formation of a functional catalytic pocket.
18 min
Specificity, efficiency, and isoenzymes
Understand substrate recognition, catalysis, and enzyme variation across tissues.
20 min
Naming, classifying, and using enzymes
Decode an enzyme name, distinguish EC classes, and connect enzymology with applications.
22 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
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.
Allosteric enzymes
The structural, kinetic, and regulatory principles that let certain enzymes control a metabolic pathway.