Enzyme Terminologies Quiz
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Questions and Answers

What is an enzyme?

A compound, usually a protein, that acts as a catalyst for biochemical reactions.

What does the term 'inhibition' refer to in enzyme activity?

It refers to the process that makes an active enzyme less active or inactive.

The substance upon which the enzyme acts is called the ______.

substrate

What is a coenzyme?

<p>A non-protein organic molecule that acts as a cofactor in a conjugated enzyme.</p> Signup and view all the answers

What is an apoenzyme?

<p>The protein part of an enzyme.</p> Signup and view all the answers

Define 'active site' in enzymes.

<p>A specific portion of the enzyme where a substrate binds during a reaction.</p> Signup and view all the answers

What are the primary characteristics of enzymes? (Select all that apply)

<p>Predominantly protein in nature</p> Signup and view all the answers

The lock-and-key model suggests that the active site has a flexible shape.

<p>False</p> Signup and view all the answers

What is an inhibitor?

<p>A compound that slows down the rate of a reaction.</p> Signup and view all the answers

What is the holoenzyme?

<p>Apoenzyme plus prosthetic group</p> Signup and view all the answers

Study Notes

Enzyme Basics

  • Enzymes are biological catalysts primarily composed of proteins, facilitating biochemical reactions without being consumed.
  • Inhibition refers to the process that decreases or halts enzyme activity.
  • Substrates are the specific compounds on which enzymes act to produce products.

Characteristics of Enzymes

  • Predominantly proteins, with exceptions like ribozymes (made of RNA).
  • Increase reaction rates by factors of 10 to 20 times.
  • Commonly end with the suffix "-ase" (e.g., urease, sucrase, lipase).

Enzyme Structure

  • Conjugated enzymes consist of a protein (apoenzyme) and an additional non-protein part.
  • Cofactors, such as minerals (e.g., Zn, Mg), are non-protein components vital for enzyme activity.
  • Coenzymes are non-protein organic molecules (often B vitamins) that enhance enzyme function.
  • Prosthetic groups are tightly bound cofactors/coenzymes in the enzyme structure.
  • Holoenzyme is the complete functioning enzyme formed by the apoenzyme and prosthetic group.

Mechanism of Enzyme Activity

  • The active site is the specific region where substrates bind and reactions occur.
  • The enzyme-substrate complex is formed in the first step and is reversible.
  • The conversion of the enzyme-substrate complex into products regenerates the enzyme.

Specificity of Enzymes

  • Bond specificity refers to the enzyme acting on specific bonds in substrates.
  • Group specificity allows enzymes to target only specific functional groups on molecules.
  • Substrate specificity indicates that enzymes can act on particular substrate types.
  • Optical specificity means enzymes can differentiate between isomers, such as L and D amino acids.
  • Geometrical specificity denotes that enzyme activity depends on the shape of the substrate.
  • Cofactor specificity highlights that certain enzymes require particular cofactors to function.

Activation and Regulation

  • Activation refers to processes that increase enzyme activity.
  • Allosteric sites on enzymes allow for binding of activators or inhibitors to regulate enzymatic activity.
  • Inhibitors are compounds that slow down or stop enzyme function by binding to the enzyme.

Catalysis Models

  • The Lock-and-Key Model posits that enzymes have a rigid active site shape that only fits specific substrate geometries.
  • Collision Theory explains that reactions require effective collisions between reactants, overcoming activation energy barriers.
  • Transition State Theory focuses on the transformation of reactants into products through a transient state during the reaction.

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Description

Test your knowledge on enzyme terminologies and characteristics in this quiz. Explore concepts such as inhibition and the role of enzymes as biological catalysts. Perfect for students learning about biochemistry.

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