Enzymes Overview Quiz

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Questions and Answers

What is an enzyme?

An organic compound that acts as a catalyst for a biochemical reaction and increases the rate of reaction without being changed in the process.

Which of the following is NOT a feature of enzymes?

  • They can be changed in the process. (correct)
  • They are water-soluble.
  • They are very specific.
  • They enhance reaction rates.

What is a metalloenzyme?

An enzyme that is bound tightly to a metal ion and does not dissociate even after extensive purification.

An apoenzyme is the inactive form of an enzyme that requires a cofactor to become active.

<p>True (A)</p> Signup and view all the answers

What is the reactant in an enzyme-catalyzed reaction called?

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

Which of the following suffixes typically identifies an enzyme?

<p>-ase (A)</p> Signup and view all the answers

What type of reaction does a hydrolase enzyme catalyze?

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

What type of enzyme catalyzes the transfer of a functional group from one molecule to another?

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

Which of the following is NOT a subclass of transferases?

<p>Dehydrogenases (D)</p> Signup and view all the answers

Flashcards

Enzyme

An organic compound that acts as a catalyst in biochemical reactions, increasing the reaction rate without being consumed or altered.

Coenzyme

A small organic molecule that acts as a cofactor to assist an enzyme in its catalytic function.

Cofactor

A nonprotein component needed by certain enzymes for function. Can be an inorganic ion or organic molecule.

Apoenzyme

The protein part of a conjugated enzyme; inactive until combined with a cofactor.

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Holoenzyme

The complete, biologically active form of a conjugated enzyme (apoenzyme + cofactor).

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Proenzyme (Zymogen)

An inactive enzyme precursor that requires modification to become active.

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Active Site

The specific region on an enzyme where the substrate binds and the reaction occurs.

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Substrate

The reactant molecule upon which an enzyme acts.

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Catalysis

Increasing reaction rate by lowering activation energy.

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Specificity

Enzymes' ability to catalyze only specific reactions or bind only specific reactants.

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Hydrolase

Enzyme catalyzing hydrolysis reactions where water is used to break bonds.

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Oxidoreductase

Enzymes catalyzing oxidation-reduction reactions, often using coenzymes.

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Transferase

Enzyme catalyzing the transfer of a functional group from one molecule to another.

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Lyase

Enzyme catalyzing the addition or removal of groups from double bonds without hydrolysis or oxidation.

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Isomerase

Enzyme catalyzing the rearrangement of atoms within a molecule, creating isomers.

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Ligase

Enzyme catalyzing the joining of two molecules using energy from ATP.

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Enzyme Classes

Enzymes are grouped into classes based on the type of reaction they catalyze.

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Enzyme Activity Regulation

The process of controlling the rate of enzyme-catalyzed reactions to meet the cell's needs.

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Enzyme Location

The specific positions of enzymes in a cell, often crucial to their function.

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Study Notes

Enzymes

  • Enzymes are biological catalysts that speed up chemical reactions without being consumed in the process.
  • They are typically proteins, but some RNA molecules can also act as enzymes, known as ribozymes.
  • Enzymes bind to specific molecules called substrates, facilitating their conversion into products.
  • The rate of an enzyme-catalyzed reaction is higher than the rate of the uncatalyzed reaction.

Enzyme Features

  • Enzymes are highly specific, typically catalyzing only one or a small number of reactions.
  • Enzymes are subject to regulation, allowing cells to control their metabolic processes.
  • Enzymes are affected by temperature and pH, having optimal conditions for activity.
  • Enzymes do not change the equilibrium constant of a reaction.
  • Enzymes are reusable, participating in multiple rounds of catalysis.

Metalloenzymes

  • Metalloenzymes are enzymes that require a metal ion for their activity.
  • The metal ion acts as a cofactor, assisting in the catalytic process.
  • Examples of metalloenzymes include:
    • Cytochrome oxidase: contains copper and iron ions
    • Carbonic anhydrase: contains zinc ions

Apoenzymes and Cofactors

  • Apoenzymes are the inactive form of an enzyme that requires a cofactor to become active.
  • Cofactors can be inorganic ions (like metal ions) or organic molecules (like vitamins).
  • Holoenzyme is the fully active enzyme containing both the apoenzyme and the cofactor.

Substrate

  • The reactant in an enzyme-catalyzed reaction is called the substrate.
  • The substrate binds to the enzyme's active site, forming an enzyme-substrate complex.

Enzyme Nomenclature

  • Many enzymes end with the suffix -ase.
  • Examples include:
    • Lactase: breaks down lactose
    • Protease: breaks down proteins

Hydrolases

  • Hydrolases are enzymes that catalyze the hydrolysis of a chemical bond, usually by adding water.
  • They break down larger molecules into smaller ones.
  • Examples include:
    • Lipase: breaks down lipids
    • Amylase: breaks down carbohydrates

Transferases

  • Transferases catalyze the transfer of a functional group (like a phosphate group) from one molecule to another.
  • Examples include:
    • Kinases: transfer a phosphate group
    • Glycosyltransferases: transfer a sugar molecule
    • Methyltransferases: transfer a methyl group
  • Dehydrogenases are a subclass of transferases that transfer hydrogen ions and electrons.

Subclasses of Transferases

  • Phosphotransferases: transfer phosphate groups

  • Glycosyltransferases: transfer sugar molecules

  • Methyltransferases: transfer methyl groups

  • Dehydrogenases: transfer electrons and hydrogen ions

  • Acyltransferases: transfer acyl groups

  • Isomerases are NOT a subclass of transferases. They catalyze the rearrangement of atoms within a molecule, converting one isomer to another.

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