Lock and Key Model in Enzymes

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What is the Lock and Key Model?

The Lock and Key Model is a theory explaining how enzymes and substrates interact based on shape complementarity.

Who proposed the Lock and Key Model?

Emil Fischer proposed the Lock and Key Model in 1894.

How does the Lock and Key Model differ from the Induced Fit Model?

The Lock and Key Model suggests strict specificity, while the Induced Fit Model suggests flexibility in enzyme shape.

What is substrate specificity?

Substrate specificity refers to the ability of an enzyme to select and catalyze a particular substrate.

Can the Lock and Key Model explain all enzyme reactions?

No, it cannot explain all enzyme reactions as some require flexibility as proposed by the Induced Fit Model.

Why is the Lock and Key Model important?

It provides a fundamental understanding of enzyme specificity and catalysis.

What is an active site?

An active site is the region on an enzyme where substrate molecules bind and undergo a chemical reaction.

How does enzyme specificity benefit organisms?

It ensures precise and efficient biochemical reactions necessary for life processes.

What role does shape play in the Lock and Key Model?

Shape determines the ability of the substrate to bind to the enzyme's active site.

How did Emil Fischer test the Lock and Key Model?

Emil Fischer used experiments with sugars and enzymes to demonstrate substrate specificity.

What are enzymes?

Enzymes are biological catalysts that speed up chemical reactions in living organisms.

What is an example of enzyme specificity?

The enzyme sucrase specifically breaks down the sugar sucrose into glucose and fructose.

In what field is the Lock and Key Model particularly useful?

It is particularly useful in the fields of biochemistry and pharmacology.

What limitation does the Lock and Key Model have?

It does not account for changes in enzyme shape during substrate binding.

How can enzyme inhibitors affect enzymes functioning according to the Lock and Key Model?

Inhibitors can block the active site, preventing substrate binding and enzyme functionality.

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