Comparison between Lock and Key Model and Induced Fit Model

Let me share with you a Comparison between Lock and Key Model and Induced Fit Model.

 

Aspect Lock and Key Model Induced Fit Model
Introduction According to this model, Substrate fits into the active site of an enzyme just like a key fits into a lock. According to this model, Substrate induces a conformational change in the enzyme structure.
Fit Substrate and active site have a complementary shape. Initial fit may not be perfect; enzyme adjusts its shape.
Specificity Highly specific; each enzyme has a unique active site. Specific, but initial fit is less strict.
Enzyme Shape Enzyme shape is rigid and does not change during catalysis. Enzyme undergoes a conformational change upon substrate binding.
Binding Strength Binding is strong and does not change during catalysis. Initial binding is weak, strengthened during induced fit.
Energy Requirements No significant energy is required for the substrate to bind. Energy is required for the enzyme to change its shape.
Analogy Like a key fitting into a lock. Like a glove adjusting its shape to fit a hand.
Flexibility Enzyme active site is inflexible. Enzyme active site is flexible and dynamic.
Time Scale Binding is rapid and specific. Binding and catalysis may take slightly more time.
Examples ·        Amylase

·        Trypsin

·        DNA polymerase

·        RIbonuclease