Enzymes: Biological Catalysts

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Questions and Answers

What is the primary role of enzymes within living cells?

  • To serve as structural components.
  • To accelerate metabolic reaction rates. (correct)
  • To store genetic information.
  • To be consumed as nutrients.

Which characteristic of an enzyme is primarily responsible for its specificity?

  • Its compatibility of shapes and charges with substrates. (correct)
  • Its sequence of amino acids.
  • Its small physical size.
  • Its ability to function at a wide range of temperatures.

Where does an enzyme bind its substrate?

  • At any location on the enzyme.
  • At a specific region called the active site. (correct)
  • Within the enzyme's secondary structure.
  • On the quaternary structure of the enzyme.

Which theory explains how an enzyme recognizes and binds to its substrate?

<p>Lock and Key theory. (D)</p> Signup and view all the answers

What does the suffix '-ase' typically indicate in a biochemical name?

<p>An enzyme. (A)</p> Signup and view all the answers

How are enzymes systematically classified?

<p>By their EC number and the type of reaction they catalyze. (C)</p> Signup and view all the answers

What is the function of hydrolases (EC 3)?

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

What primary factor regulates enzyme activity?

<p>Temperature and pH. (D)</p> Signup and view all the answers

How do enzymes affect the activation energy of a chemical reaction?

<p>They lower the activation energy. (A)</p> Signup and view all the answers

What is the function of enzyme inhibitors?

<p>To decrease reaction rates. (D)</p> Signup and view all the answers

Which is a characteristic of reversible enzyme inhibitors?

<p>They bind via non-covalent interactions. (D)</p> Signup and view all the answers

How do competitive inhibitors affect enzyme activity?

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

What is the mechanism of action of non-competitive inhibitors?

<p>They bind at a site away from the active site, altering enzyme shape. (A)</p> Signup and view all the answers

What is a proenzyme?

<p>An inactive precursor of an enzyme. (D)</p> Signup and view all the answers

How do cofactors and coenzymes assist enzymes?

<p>By carrying out the process. (C)</p> Signup and view all the answers

What is the difference between cofactors and coenzymes?

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

What is the key characteristic of metalloproteins?

<p>They contain tightly bound metal ions. (D)</p> Signup and view all the answers

Which of the following vitamins is a precursor to flavin adenine dinucleotide (FAD)?

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

Which vitamin is part of coenzyme A (CoA)?

<p>Pantothenic Acid (Vitamin B5). (B)</p> Signup and view all the answers

What is the function of ascorbic acid (Vitamin C)?

<p>Antioxidant and collagen synthesis. (C)</p> Signup and view all the answers

What defines a heterocyclic compound?

<p>A compound with one or more non-carbon atoms (heteroatoms) in a ring structure. (A)</p> Signup and view all the answers

What is a porphyrin?

<p>A pyrrole derivative ring. (C)</p> Signup and view all the answers

Which metal does heme contain?

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

What is the primary function of heme in the body?

<p>To carry oxygen in the blood. (A)</p> Signup and view all the answers

Which amino acid has an indole ring in its structure?

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

Which of the following is a pyrimidine base found in nucleic acids?

<p>Cytosine. (B)</p> Signup and view all the answers

What is a nucleoside?

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

How does a nucleotide differ from a nucleoside?

<p>A nucleotide contains one or more phosphate groups attached to the sugar. (B)</p> Signup and view all the answers

What is the role of nucleotides?

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

What type of bond links nucleotides in nucleic acids?

<p>Phosphodiester bonds. (A)</p> Signup and view all the answers

Which of the following bases is unique to DNA?

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

Which base pairs with guanine in DNA?

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

What type of sugar is found in RNA?

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

What type of nucleic acid is typically single-stranded?

<p>RNA. (C)</p> Signup and view all the answers

Which base is found in RNA but not in DNA?

<p>Uracil. (C)</p> Signup and view all the answers

What is the function of mRNA?

<p>Carries genetic information from the nucleus to the ribosome. (D)</p> Signup and view all the answers

What are the key structural differences between DNA and RNA?

<p>DNA is double-stranded and contains deoxyribose, while RNA is single-stranded and contains ribose. (D)</p> Signup and view all the answers

Which is a component of RNA nucleotides but not DNA nucleotides?

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

A researcher is studying a molecule that appears to be involved in transferring genetic information within a cell. Analysis reveals that the molecule contains ribose sugar, uracil, and is single-stranded. Which molecule is the researcher most likely studying?

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

How does an enzyme interact with its substrate to facilitate a reaction?

<p>By lowering the activation energy, forcing the reacting molecules through a different transition state. (B)</p> Signup and view all the answers

Which of the following is an example of irreversible enzyme inhibition?

<p>A substance forming a covalent bond with the enzyme, permanently altering its structure. (D)</p> Signup and view all the answers

How do coenzymes differ from cofactors in enzyme-catalyzed reactions?

<p>Coenzymes are organic molecules, often derived from vitamins, while cofactors can be either inorganic ions or organic molecules. (C)</p> Signup and view all the answers

In the systematic classification of enzymes using EC numbers, what information is provided by the first digit?

<p>The main class of reaction the enzyme catalyzes. (B)</p> Signup and view all the answers

Which of the following best describes the role of metalloproteins in enzymatic activity?

<p>They contain tightly bound metal ions at their active sites that contribute to the enzyme's catalytic function. (A)</p> Signup and view all the answers

Flashcards

Enzymes

Biological catalysts that accelerate reaction rates within living cells.

Enzyme Specificity

Enzymes enhance reaction rates without being used up.

Active Site

Region where enzymes bind substrates, promoting reactions.

EC Number Classification

Classification system for enzymes based on reaction type.

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Transferases

Transfer of chemical groups.

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Lyases

Cleavage of chemical bonds.

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Isomerases

Geometric and structural changes between isomers.

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pH and Enzyme Activity

Enzymes function optimally within specific pH ranges.

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Enzyme Inhibitors

Molecules that decrease enzyme activity.

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Reversible Inhibition

Binds via non covalent interaction. No chemical changes. Can be reversed.

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Irreversible Inhibition

Binds via covalent bond, prevents catalytic activity, irreversible.

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Competitive Inhibitors

Molecules similar to the substrate bind to the active site.

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Non-competitive inhibitors

Bind elsewhere, altering the enzyme's shape and reducing activity.

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Enzyme Activation

Converting an inactive enzyme into a metabolically active molecule.

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Cofactors and Coenzymes

Molecules required for enzyme function.

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Cofactors

Inorganic ions or organic molecules assisting enzymes.

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Coenzymes

Organic molecules that function as cofactors.

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Metalloproteins

Enzymes containing tightly metal ions at their active sites.

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Water-Soluble Vitamins

Precursors to coenzymes, participate in metabolism.

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Thiamin (Vitamin B1)

Part of thiamin pyrophosphate (TPP), decarboxylation reactions.

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Riboflavin (Vitamin B2)

Forms flavin adenine dinucleotide (FAD) and FMN, redox reactions.

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Niacin (Vitamin B3)

Part of nicotinamide adenine dinucleotide (NAD+), redox reactions.

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Pantothenic Acid (Vitamin B5)

Part of coenzyme A (CoA), energy production and lipid metabolism.

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Pyridoxine (Vitamin B6)

Converted to pyridoxal phosphate (PLP), amino acid transamination.

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Folic Acid (B9)

Forms tetrahydrofolate (THFA), nucleic acid synthesis.

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Cobalamin (Vitamin B12)

Involved in methyl group transfer.

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Vitamin C (Ascorbic Acid)

Antioxidant, collagen synthesis and biogenic amine biosynthesis.

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Heterocyclic Compounds

Organic compounds with heteroatoms in a ring structure.

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Pyrrole Derivatives (Porphyrins)

Pyrrole rings form key biological compounds.

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Heme

Iron-porphyrin complex, red color of arterial blood.

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Indole

A fused-ring system, found in tryptophan and its derivatives.

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Purines (Adenine, Guanine)

Bases found in nucleic acids.

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Pyrimidines (Cytosine, Thymine, Uracil)

Bases found in nucleic acids.

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Nucleosides

Nitrogenous base linked to sugar.

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Nucleotides

Nucleoside with one or more phosphate groups.

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Nucleotide Function

Building blocks for DNA/RNA, energy source.

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Nucleic Acids (DNA and RNA)

Polymers of nucleotides linked by phosphodiester bonds.

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DNA (Deoxyribonucleic Acid)

Double-stranded helix.

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DNA Base Pairing

A-T, G-C.

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RNA (Ribonucleic Acid)

Single-stranded.

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RNA Functions

mRNA (messenger), rRNA (ribosomal), tRNA (transfer).

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DNA vs. RNA

DNA – double stranded, very long.

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Study Notes

Enzymes: Biological Catalysts

  • Enzymes are biological catalysts accelerating reactions in living cells, essential for metabolic processes.
  • Enzymes exhibit substrate specificity due to complementary shapes and characteristics between the enzyme and its substrates.
  • Substrates bind to enzymes at the active site, forming an enzyme-substrate complex.

Enzyme-Substrate Interaction

  • The active site, a pocket within the enzyme's structure, binds to the substrate.
  • Specificity is explained by the "Lock and Key" and "Induced-fit" theories.

Enzyme Nomenclature and Classification

  • Enzyme names usually end in "-ase" and are classified using an EC (Enzyme Commission) number based on reaction type.
  • EC numbers categorize enzymes into main classes, including 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 is composed of four digits indicating class, subclass, sub-subclass, and serial number.

Enzyme Properties and Regulation

  • Enzymes are excellent catalysts regulated by temperature, pH, and additives.
  • Enzymes lower activation energy by guiding reacting molecules through a different transition state.
  • Enzyme activity is affected by pH, temperature, inhibitors, and activators.

Enzyme Inhibition

  • Inhibitors modulate enzyme activity, with reversible inhibitors binding via non-covalent interactions and irreversible inhibitors binding via covalent bonds.
  • Competitive inhibitors bind to the active site; non-competitive inhibitors bind elsewhere, altering the enzyme's shape.

Enzyme Activation

  • Enzymes may be activated by ions like Ca2+ and Mg2+, cofactors, coenzymes, or proenzyme conversion.
  • Activators bind to enzyme molecules, boosting metabolic activity.

Cofactors and Coenzymes: Enzyme Helpers

  • Some enzymes need additional molecules, either cofactors or coenzymes, to function.
  • Cofactors are inorganic ions or organic molecules assisting enzymes.
  • Coenzymes are organic molecules that act as cofactors, often derived from vitamins.
  • Metalloenzymes contain tightly bound metal ions at their active sites.

Water-Soluble Vitamins as Coenzyme Precursors

  • Many 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): Forms thiamin pyrophosphate (TPP), which is involved in decarboxylation reactions.
  • Riboflavin (Vitamin B2): Forms flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), used in redox reactions.
  • Niacin (Vitamin B3): Forms nicotinamide adenine dinucleotide (NAD+) and NADP+, used in redox reactions.
  • Pantothenic Acid (Vitamin B5): Forms 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: Transfer reactions involving carboxyl-groups.
  • Folic Acid (B9): Synthesis of nucleic acid using tetrahydrofolate (THFA).
  • Cobalamin (Vitamin B12): Transfer of methyl groups.
  • Vitamin C (Ascorbic Acid): Functions as an antioxidant and participates in collagen synthesis and biogenic amine biosynthesis.

Heterocyclic Compounds

  • Heterocyclic compounds are organic compounds where one or more carbon atoms in a ring structure are replaced by heteroatoms like oxygen, nitrogen, or sulfur.
  • Classified by the number of atoms in the ring, type of heteroatoms, and number of rings.

Biologically Important Heterocyclic Examples

  • Pyrrole derivatives (Porphyrins): Form the building blocks of compounds in biologic processes.
  • Heme: An iron-porphyrin complex that gives arterial blood its red color and is found in hemoglobin.
  • Indole: Found in tryptophan and its derivatives like serotonin and is a fused-ring system.
  • Pyrimidines: Cytosine, Thymine, and Uracil are bases found in nucleic acids.
  • Purines: Adenine, and Guanine are bases found in nucleic acids.

Nucleosides and Nucleotides

  • Nucleosides: A nitrogenous base (purine or pyrimidine) linked to a sugar (ribose or deoxyribose) via a glycosidic bond.
  • Nucleotides: Nucleosides with one or more phosphate groups attached to the sugar.
  • Nucleotides serve as building blocks for DNA and RNA, energy sources (ATP), second messengers, and intracellular signaling switches.

Nucleic Acids: DNA and RNA

  • Polymers of nucleotides linked by phosphodiester bonds store information for cellular growth and reproduction.
  • Two types include deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).

DNA (Deoxyribonucleic Acid)

  • DNA is a double-stranded helix containing deoxyribose sugar.
  • DNA contains the bases Adenine (A), Guanine (G), Cytosine (C), and Thymine (T).
  • Base pairing: A-T, G-C is held together by purine-pyrimidine base pairs connected by hydrogen bonds.
  • Primary structure: Units of 2-deoxy-ribose and phosphate alternate in the backbone.

RNA (Ribonucleic Acid)

  • RNA is single-stranded and contains ribose sugar.
  • RNA contains the bases Adenine (A), Guanine (G), Cytosine (C), and Uracil (U).
  • Functions: mRNA (messenger), rRNA (ribosomal), tRNA (transfer).

Key Differences Between DNA and RNA

  • RNA is single-stranded and shorter; DNA is double-stranded and very long.
  • DNA nucleotides: Deoxyribose, phosphate, and one of four nitrogenous bases (Adenine, Guanine, Thymine, Cytosine).
  • RNA nucleotides: Ribose, phosphate, and one of four nitrogenous bases (Adenine, Guanine, Uracil, Cytosine).

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