Enzymes: Biological Catalysts

Choose a study mode

Play Quiz
Study Flashcards
Spaced Repetition
Chat to Lesson

Podcast

Play an AI-generated podcast conversation about this lesson

Questions and Answers

Which statement best describes the role of enzymes in biochemical reactions?

  • Enzymes increase the activation energy required for the reaction.
  • Enzymes alter the equilibrium of the reaction to favor product formation.
  • Enzymes act as biological catalysts, accelerating reaction rates. (correct)
  • Enzymes are consumed during the reaction to provide energy.

Enzyme specificity is primarily determined by what?

  • The pH and temperature of the environment.
  • The concentration of the enzyme in the reaction mixture.
  • The presence of cofactors or coenzymes.
  • The complementary shapes and characteristics between the enzyme and its substrates. (correct)

Which of the following best describes the 'Lock and Key' theory and 'Induced-fit' theory in enzyme-substrate interactions?

  • The 'Lock and Key' theory applies to competitive inhibition, while the 'Induced-fit' theory applies to non-competitive inhibition.
  • The 'Lock and Key' theory involves a flexible active site that molds around the substrate, while the 'Induced-fit' theory describes a rigid active site.
  • Both theories describe the same mechanism of enzyme-substrate interaction but differ in terminology.
  • The 'Lock and Key' theory describes a rigid active site that perfectly fits the substrate, while the 'Induced-fit' theory involves a conformational change in the enzyme upon substrate binding. (correct)

An enzyme is classified as EC 3.2.1.1. What type of reaction does this enzyme catalyze?

<p>Hydrolysis of chemical bonds (B)</p> Signup and view all the answers

How do enzymes enhance reaction rates?

<p>By lowering the activation energy required for the reaction. (D)</p> Signup and view all the answers

Why do changes in pH and temperature affect enzyme activity?

<p>They disrupt the three-dimensional structure of the enzyme, affecting its active site. (C)</p> Signup and view all the answers

Which of the following describes a reversible enzyme inhibitor?

<p>It binds to the enzyme through non-covalent interactions and can be displaced. (A)</p> Signup and view all the answers

How do competitive enzyme inhibitors affect enzyme activity?

<p>They bind to the active site, preventing substrate binding. (A)</p> Signup and view all the answers

How do non-competitive inhibitors affect enzyme activity?

<p>By binding to the enzyme at a site different from the active site, altering its conformation. (B)</p> Signup and view all the answers

Which of the following is an example of enzyme activation?

<p>The conversion of a zymogen into an active enzyme. (A)</p> Signup and view all the answers

What is the general role of cofactors and coenzymes in enzyme function?

<p>They are additional molecules that are needed for some enzymes to function. (D)</p> Signup and view all the answers

Which of the following is an example of a cofactor?

<p>A metal ion such as $Mg^{2+}$ (A)</p> Signup and view all the answers

What is the primary difference between a cofactor and a coenzyme?

<p>Cofactors are inorganic ions, while coenzymes are organic molecules. (D)</p> Signup and view all the answers

What is the role of metalloproteins in enzyme catalysis?

<p>They contain tightly bound metal ions at their active sites that aid in catalysis. (C)</p> Signup and view all the answers

If a patient is deficient in thiamin (Vitamin B1), which enzymatic reaction might be impaired?

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

Which vitamin is essential for the formation of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN)?

<p>Riboflavin (Vitamin B2) (C)</p> Signup and view all the answers

Niacin (Vitamin B3) plays a critical role in which type of biochemical reactions?

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

Pantothenic acid is a component of which coenzyme?

<p>Coenzyme A (CoA) (D)</p> Signup and view all the answers

Pyridoxine (Vitamin B6) is important for which type of biochemical reaction?

<p>Amino acid transamination (C)</p> Signup and view all the answers

Cobalamin (Vitamin B12) is directly involved in which metabolic process?

<p>Methyl group transfer (A)</p> Signup and view all the answers

Vitamin C (Ascorbic Acid) acts as an antioxidant with what addition role in the body?

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

What is a general characteristic of heterocyclic compounds?

<p>They contain at least one atom other than carbon or hydrogen in a ring structure. (B)</p> Signup and view all the answers

What is the main function of porphyrins in biological systems?

<p>To serve as building blocks for biologically important compounds like heme. (C)</p> Signup and view all the answers

What is the role of heme in the body?

<p>To give blood its red color and aid in oxygen transport (B)</p> Signup and view all the answers

Which of the following molecules is a derivative of indole?

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

What is the major structural difference between purines and pyrimidines?

<p>Purines contain a double-ring structure, while pyrimidines have a single-ring structure. (D)</p> Signup and view all the answers

Which of the following best describes a nucleoside?

<p>A nitrogenous base linked to a sugar. (D)</p> Signup and view all the answers

What distinguishes a nucleotide from a nucleoside?

<p>A nucleotide contains a phosphate group, while a nucleoside does not. (D)</p> Signup and view all the answers

What are the primary functions of nucleotides in cells?

<p>Building blocks for DNA and RNA and intracellular signaling. (C)</p> Signup and view all the answers

What type of bond links nucleotides together to form nucleic acids?

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

Which nitrogenous base is unique to DNA?

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

What is the base pairing rule in DNA?

<p>A-T, G-C (C)</p> Signup and view all the answers

How does the sugar component differ between DNA and RNA?

<p>DNA contains deoxyribose, while RNA contains ribose. (A)</p> Signup and view all the answers

What is the key structural difference between DNA and RNA molecules?

<p>DNA is typically double-stranded, while RNA is typically single-stranded. (A)</p> Signup and view all the answers

Which of the following is a function of mRNA?

<p>To serve as a template for protein synthesis (B)</p> Signup and view all the answers

Which of the following molecules correctly illustrates the key differences between DNA and RNA nucleotides:

<p>DNA: Deoxyribose, Thymine; RNA: Ribose, Uracil (A)</p> Signup and view all the answers

Which of the following best explains why enzymes exhibit high specificity for their substrates?

<p>The active site of the enzyme has a shape and chemical properties that are highly complementary to the substrate. (C)</p> Signup and view all the answers

An enzyme is known to catalyze the transfer of a phosphate group from ATP to a substrate. According to the EC classification system, to which class does this enzyme belong?

<p>Transferases (EC 2) (D)</p> Signup and view all the answers

How do irreversible enzyme inhibitors differ fundamentally from reversible inhibitors in their mechanism of action?

<p>Irreversible inhibitors permanently alter the enzyme through covalent bond formation, whereas reversible inhibitors bind through non-covalent interactions. (D)</p> Signup and view all the answers

Which of the following best describes the role of a coenzyme in an enzymatic reaction?

<p>A coenzyme is an organic molecule that assists the enzyme in catalyzing a reaction, often by carrying chemical groups. (D)</p> Signup and view all the answers

How does Vitamin B1 (Thiamin) contribute to enzyme function?

<p>It is part of thiamin pyrophosphate (TPP), crucial in decarboxylation reactions. (A)</p> Signup and view all the answers

Flashcards

Enzymes

Biological catalysts that accelerate reaction rates within living cells.

Enzyme Specificity

The characteristic of enzymes being selective in the reactions they catalyze.

Enzyme Active Site

A specific region on an enzyme where substrates bind.

Enzyme Names

Indicate enzyme function with the suffix '-ase'.

Signup and view all the flashcards

EC Number

System for classifying enzymes based on reaction type.

Signup and view all the flashcards

Enzyme Catalysis

Enzymes decrease activation energy, speeding up reactions.

Signup and view all the flashcards

Enzyme Inhibitors

Molecules that decrease enzyme activity.

Signup and view all the flashcards

Reversible Inhibition

Binds via non covalent interaction, reversible.

Signup and view all the flashcards

Irreversible Inhibition

Binds via covalent bond, inhibitor binds to the substrate.

Signup and view all the flashcards

Enzyme Activators

Molecules that increase enzyme activity.

Signup and view all the flashcards

Cofactors and Coenzymes

Additional molecules required by some enzymes to function.

Signup and view all the flashcards

Cofactors

Inorganic ions that assist enzymes.

Signup and view all the flashcards

Coenzymes

Organic molecules that function as cofactors.

Signup and view all the flashcards

Metalloproteins

Enzymes containing tightly bound metal ions at their active sites.

Signup and view all the flashcards

Water-Soluble Vitamins

Many water-soluble vitamins are precursors to coenzymes.

Signup and view all the flashcards

Thiamin (Vitamin B1)

Part of thiamin pyrophosphate (TPP), involved in decarboxylation reactions.

Signup and view all the flashcards

Riboflavin (Vitamin B2)

Forms flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN); used in redox reactions.

Signup and view all the flashcards

Niacin (Vitamin B3)

Part of nicotinamide adenine dinucleotide (NAD+) and NADP+, used in redox reactions.

Signup and view all the flashcards

Pantothenic Acid (Vitamin B5)

Part of coenzyme A (CoA); involved in energy production and lipid/amino acid metabolism.

Signup and view all the flashcards

Pyridoxine (Vitamin B6)

Converted to pyridoxal phosphate (PLP); involved in amino acid transamination and decarboxylation.

Signup and view all the flashcards

Folic Acid (B9)

forms tetrahydrofolate (THFA), used in nucleic acid synthesis.

Signup and view all the flashcards

Cobalamin (Vitamin B12)

Involved in methyl group transfer.

Signup and view all the flashcards

Vitamin C (Ascorbic Acid)

Acts as an antioxidant and is involved in collagen synthesis and biogenic amine biosynthesis.

Signup and view all the flashcards

Heterocyclic Compounds

Organic compounds with atoms other than C or H in a ring.

Signup and view all the flashcards

Heterocyclic Classification (Number of Atoms)

Classification based on the number of atoms in the ring.

Signup and view all the flashcards

Pyrrole Derivatives (Porphyrins)

Pyrrole rings form the building blocks.

Signup and view all the flashcards

Heme

The iron-porphyrin complex responsible for the red color of arterial blood, found in hemoglobin.

Signup and view all the flashcards

Nucleosides

A nitrogenous base linked to a sugar (ribose or deoxyribose) via a glycosidic bond.

Signup and view all the flashcards

Nucleotides

A nucleoside with one or more phosphate groups attached to the sugar.

Signup and view all the flashcards

Nucleic Acids (DNA and RNA)

Polymers of nucleotides linked by phosphodiester bonds.

Signup and view all the flashcards

DNA (Deoxyribonucleic Acid)

Double-stranded helix with deoxyribose sugar.

Signup and view all the flashcards

RNA (Ribonucleic Acid)

Single-stranded nucleic acid with ribose sugar.

Signup and view all the flashcards

Bases in DNA

Different nitrogenous bases in DNA

Signup and view all the flashcards

Bases in RNA

Different nitrogenous bases in RNA

Signup and view all the flashcards

Study Notes

Enzymes: Biological Catalysts

  • Enzymes are biological catalysts accelerating reaction rates in living cells.
  • Enzymes exhibit substrate specificity, enhancing reaction rates without being used up.
  • This specificity arises from complementary shapes, charges, and hydrophilic/hydrophobic characteristics.
  • Enzymes bind substrates at the active site, forming an enzyme-substrate complex, a pocket that is part of the enzyme's tertiary/quaternary structure.
  • The "Lock and Key" and "Induced-fit" theories explain enzyme specificity.
  • Enzymes are named with the suffix "-ase" and classified with an EC number based on reaction type.
  • Enzymes are classified into main classes that include Oxidoreductases (EC 1), Transferases (EC 2), Hydrolases (EC 3), Lyases (EC 4), Isomerases (EC 5), Ligases (EC 6), and Translocases (EC 7).
  • The EC number has four digits indicating enzyme class, subclass, sub-subclass, and serial number.
  • Enzymes are excellent catalysts regulated by temperature, pH, and additives.
  • They lower activation energy by forcing molecules through a different transition state.
  • Enzyme activity is affected by pH, temperature, and molecules like inhibitors (decrease activity) and activators (increase activity).
  • Enzyme activity can be modulated through inhibition.
  • Reversible inhibition involves non-covalent interactions, while irreversible inhibition involves covalent bonds.
  • Competitive inhibitors bind to the active site; non-competitive inhibitors bind elsewhere, altering the enzyme's shape and reducing activity.
  • Enzymes can be activated by ions (Ca2+, Mg2+), cofactors, coenzymes, or conversion of a proenzyme.

Cofactors and Coenzymes: Enzyme helpers

  • Some enzymes need additional molecules to function, referred to as cofactors or coenzymes.
  • Cofactors are inorganic ions or organic molecules that assist enzymes.
  • Coenzymes are organic molecules functioning as cofactors, often derived from vitamins.
  • Metalloproteins are enzymes with tightly bound metal ions at their active sites.
  • Water-soluble vitamins are precursors to coenzymes, including B vitamins (Thiamin, Riboflavin, Niacin, Pantothenic Acid, Pyridoxine, Biotin, Folic Acid, Cobalamin) and Vitamin C. -Thiamin (Vitamin B1): Part of thiamin pyrophosphate (TPP), is involved in decarboxylation reactions.
  • Riboflavin (Vitamin B2): Forms flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), used in redox reactions.
  • Niacin (Vitamin B3): Part of nicotinamide adenine dinucleotide (NAD+) and NADP+, used in redox reactions.
  • Pantothenic Acid (Vitamin B5): Part of coenzyme A (CoA), involved in energy production and lipid/amino acid metabolism.
  • Pyridoxine (Vitamin B6): Converted to pyridoxal phosphate (PLP), involved in amino acid transamination and decarboxylation.
  • Biotin: Involved in carboxyl-group transfer reactions.
  • Folic Acid (B9): Forms tetrahydrofolate (THFA), used in nucleic acid synthesis.
  • Cobalamin (Vitamin B12): Involved in methyl group transfer.
  • Vitamin C (Ascorbic Acid): Acts as an antioxidant and is involved in collagen synthesis and biogenic amine biosynthesis.

Heterocyclic Compounds: Cyclic structures

  • Heterocyclic compounds are organic compounds with one or more carbon atoms in a ring structure replaced by a heteroatom (O, N, or S).
  • Heterocycles are classified based on the number of atoms in the ring, type of heteroatoms, and the number of rings (monocyclic/polycyclic).
  • Pyrrole derivatives (Porphyrins) form building blocks of biologically important compounds.
  • Heme is an iron-porphyrin complex responsible for the red color of arterial blood.
  • Indole is a fused-ring system found in tryptophan and its derivatives like serotonin.
  • Pyrimidines (Cytosine, Thymine, Uracil) and purines (Adenine, Guanine) are bases found in nucleic acids.

Nucleosides, Nucleotides, and Nucleic Acids: Genetic components

  • Nucleosides: A nitrogenous base (purine or pyrimidine) linked to a sugar (ribose or deoxyribose) via a glycosidic bond.
  • Nucleotides: A nucleoside with one or more phosphate groups attached to the sugar.
  • Nucleotides are building blocks for DNA and RNA, an intracellular energy source (ATP), and function as second messengers and intracellular signaling switches.
  • Nucleic acids (DNA and RNA) are polymers of nucleotides linked by phosphodiester bonds and store information for cellular growth and reproduction.
  • DNA (Deoxyribonucleic Acid) is a double-stranded helix containing deoxyribose sugar with bases Adenine (A), Guanine (G), Cytosine (C), and Thymine (T), with base pairing A-T and G-C.
  • RNA (Ribonucleic Acid) is single-stranded, containing ribose sugar with bases Adenine (A), Guanine (G), Cytosine (C), and Uracil (U).
  • RNA functions as mRNA (messenger), rRNA (ribosomal), and tRNA (transfer).

DNA vs. RNA: Key differences

  • RNA is single-stranded and shorter, while DNA is double-stranded and very long.
  • DNA nucleotides contain deoxyribose, phosphate, and one of the nitrogenous bases Adenine, Guanine, Thymine, or Cytosine; RNA nucleotides contain ribose, phosphate, and one of the nitrogenous bases Adenine, Guanine, Uracil, or Cytosine.

Studying That Suits You

Use AI to generate personalized quizzes and flashcards to suit your learning preferences.

Quiz Team

Related Documents

More Like This

Enzymes and Catalysis
30 questions

Enzymes and Catalysis

BoomingCotangent avatar
BoomingCotangent
Catalysis Mechanisms in Enzymes
25 questions
Use Quizgecko on...
Browser
Browser