Enzymes: Biological Catalysts

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Questions and Answers

What characteristic of enzymes is most directly responsible for their ability to catalyze specific reactions?

  • Their quaternary structure.
  • The presence of metallic cofactors.
  • The complementary shape and charge distribution of their active site. (correct)
  • Their sensitivity to changes in temperature.

Which class of enzymes is responsible for catalyzing oxidation-reduction reactions?

  • Hydrolases
  • Isomerases
  • Oxidoreductases (correct)
  • Transferases

How do enzymes affect the activation energy of a reaction?

  • By increasing the temperature of the reaction.
  • By increasing the kinetic energy of the molecules.
  • By directly providing energy to the reactants.
  • By forcing the reacting molecules through a different transition state. (correct)

What type of enzyme inhibition involves the inhibitor binding to a site other than the active site, thus altering enzyme conformation?

<p>Non-competitive inhibition (B)</p> Signup and view all the answers

Which of the following is NOT a common method of enzyme activation?

<p>Increasing the temperature well beyond its optimum range (A)</p> Signup and view all the answers

Which of the following best describes the role of coenzymes?

<p>They are organic molecules, often derived from vitamins, that assist in enzyme function. (A)</p> Signup and view all the answers

Which vitamin is a precursor to coenzyme A (CoA), vital for energy production and lipid/amino acid metabolism?

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

What is a key structural feature of heterocyclic compounds?

<p>They include one or more rings where at least one atom in the ring is not carbon or hydrogen. (B)</p> Signup and view all the answers

What is the role of the iron-porphyrin complex known as heme?

<p>It is responsible for the red color of arterial blood and oxygen transport. (A)</p> Signup and view all the answers

Which of the following is a key difference between a nucleoside and a nucleotide?

<p>A nucleoside contains a nitrogenous base and a sugar, while a nucleotide also includes one or more phosphate groups. (C)</p> Signup and view all the answers

In DNA, which of the following base pairings is correct?

<p>Adenine pairs with Thymine (A-T) (C)</p> Signup and view all the answers

What is the primary structural difference between RNA and DNA?

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

What role do transferases (EC 2) play in enzymatic reactions?

<p>Transferring chemical groups. (D)</p> Signup and view all the answers

According to the 'lock and key' theory of enzyme specificity, what is the relationship between an enzyme and its substrate?

<p>The enzyme and substrate have a complementary fit. (A)</p> Signup and view all the answers

If an enzyme's activity is most efficient at a specific pH, what would happen if the pH is drastically altered?

<p>The enzyme's structure might change, altering or eliminating its activity. (D)</p> Signup and view all the answers

Which type of inhibition involves the inhibitor permanently binding to the enzyme, often through covalent bonds?

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

What is the main function of ligases (EC 6) in biochemical reactions?

<p>Joining two compounds together, coupled with ATP hydrolysis. (C)</p> Signup and view all the answers

How do competitive inhibitors affect enzyme activity when substrate concentration increases?

<p>Their inhibitory effect decreases as the substrate concentration increases. (D)</p> Signup and view all the answers

What is the role of metalloproteins in enzyme function?

<p>They contain tightly bound metal ions that assist in catalysis at the active site. (D)</p> Signup and view all the answers

Which water-soluble vitamin is a component of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN)?

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

What is the role of Vitamin C (Ascorbic Acid) in biological systems?

<p>It acts as an antioxidant and is involved in collagen synthesis. (C)</p> Signup and view all the answers

What characteristic defines lyases (EC 4) as a distinct class of enzymes?

<p>They catalyze cleavage of chemical bonds without hydrolysis or oxidation. (D)</p> Signup and view all the answers

How do translocases (EC 7) facilitate biological processes?

<p>By transporting substances across biological membranes. (C)</p> Signup and view all the answers

In the context of enzyme regulation, what is the role of an activator?

<p>To increase the enzyme's activity by binding to the enzyme molecule. (D)</p> Signup and view all the answers

Which of the following vitamins is essential for carboxylation reactions?

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

Which of the following best describes the structure of DNA?

<p>Double-stranded helix containing deoxyribose sugar. (D)</p> Signup and view all the answers

If a molecule has a structure containing a fused-ring system and is found in tryptophan, what type of compound it is likely to be?

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

Which function is associated with nucleic acids (DNA and RNA)?

<p>Storing and transmitting genetic information. (A)</p> Signup and view all the answers

What is the effect of a non-competitive inhibitor on the enzyme's activity?

<p>It binds to a site other than the active site, changing the enzyme's shape and reducing its activity. (A)</p> Signup and view all the answers

Which class of enzymes catalyzes the joining of two large molecules by forming a new chemical bond, often with accompanying ATP hydrolysis?

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

Which of the following is a characteristic feature of transfer RNA (tRNA)?

<p>It transfers amino acids to the ribosome for protein synthesis. (A)</p> Signup and view all the answers

What role does pyridoxal phosphate (PLP), derived from Pyridoxine (Vitamin B6) play in metabolic processes?

<p>Involved in amino acid transamination and decarboxylation reactions. (D)</p> Signup and view all the answers

If an enzyme is described as having substrate specificity, what does this signify?

<p>The enzyme only acts on a specific substrate or a small number of structurally related substrates. (C)</p> Signup and view all the answers

Which of the following describes the function of isomerases (EC 5)?

<p>Rearranging atoms within a molecule to form isomers. (B)</p> Signup and view all the answers

Which of the following best describes why understanding enzymes, cofactors, heterocyclic compounds, nucleotides, and nucleic acids are essential?

<p>Understanding their structure, function and interactions is crucial for comprehending biochemical processes and developing new therapies for diseases. (C)</p> Signup and view all the answers

Which compound does NOT represent a base incorporated into the structure of RNA?

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

How does the induced-fit theory refine the 'lock and key' model of enzyme-substrate interaction?

<p>It proposes the enzyme's active site adjusts to optimally bind the substrate. (A)</p> Signup and view all the answers

If an enzyme is active in the small intestine (pH 8) but not in the stomach (pH 2), what is the most likely explanation for its inactivity in the stomach?

<p>The low pH denatures the enzyme, altering its structure. (B)</p> Signup and view all the answers

How do metalloenzymes utilize metal ions in their catalytic mechanisms?

<p>To directly participate in redox reactions or bind and orient substrates. (B)</p> Signup and view all the answers

How do water-soluble vitamins function as precursors to coenzymes?

<p>By being converted into coenzymes that assist in enzymatic reactions. (D)</p> Signup and view all the answers

How do nucleic acids, such as DNA and RNA, store and transmit genetic information?

<p>By encoding genetic information in the sequence of their nucleotide bases. (A)</p> Signup and view all the answers

Flashcards

Enzymes

Biological catalysts accelerating reaction rates in living cells.

Enzyme Specificity

Enzymes are specific to the substrates they bind to.

Active Site

Region of an enzyme where substrates bind to facilitate a reaction.

EC Number

Enzyme commission number classifies enzymes based on reaction type.

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Inhibitors

Molecules decreasing that decrease activity of enzyme molecules.

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Reversible inhibition

Binds via non-covalent interaction, no chemical changes, and can be reversed

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Irreversible inhibition

Binds via covalent bond and inhibits catalytic activity of enzyme. Irreversibility stems from strong covalent bonding

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Competitive Inhibitors

Inhibitors binding to active site, preventing substrate binding.

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Non-competitive reversible inhibitors

Molecules NOT like the substrate in shape, but bind with the enzyme.

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Activation

Ions, cofactors, coenzymes and conversion of a proenzyme.

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Cofactors/Coenzymes

Additional molecules required by some enzymes to function.

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Cofactors

Inorganic ions/organic molecules assisting enzymes.

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Coenzymes

Function as cofactors (may be certain amino acids, nitrogenous bases, and vitamins).

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Metalloproteins

Enzymes containing tightly bound metal ions at their active sites.

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Water-Soluble Vitamins

Derivatives of water-soluble vitamins play role of coenzymes and participate in metabolism of organism.

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Thiamin (Vitamin B1)

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

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Riboflavin (Vitamin B2)

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

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Niacin (Vitamin B3)

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

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Pantothenic Acid (Vitamin B5)

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

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Pyridoxine (Vitamin B6)

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

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Biotin

Involved in carboxyl-group transfer reactions.

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Folic Acid (B9)

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

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Cobalamin (Vitamin B12)

Involved in methyl group transfer.

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Vitamin C (Ascorbic Acid)

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

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Heterocyclic Compounds

Organic compounds with heteroatoms (not C or H) in a ring structure.

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Porphyrins

Pyrrole rings form the building blocks of several biologically important compounds.

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Heme

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

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Indole

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

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Pyrimidines

Bases found in nucleic acids.

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Purines

Bases found in nucleic acids.

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Nucleosides

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

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Nucleotide Function

building blocks for DNA and RNA, intracellular source of energy, second messengers, intracellular signalling switches

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Nucleic Acids

Polymers of nucleotides linked by phosphodiester bonds to store information for cellular growth and reproduction

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DNA

Double-stranded helix containing deoxyribose sugar with bases A, G, C, T

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RNA

Single-stranded containing ribose sugar with bases A, G, C, U

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Study Notes

Enzymes: Biological Catalysts

  • Enzymes are biological catalysts that accelerate reaction rates in living cells.
  • Enzymes are essential for almost every chemical reaction within cells.
  • Enzymes exhibit substrate specificity, enhancing reaction rates without being consumed.
  • Enzyme specificity comes from complementary shapes and characteristics between the enzyme and its substrate.
  • Enzymes bind substrates at the active site, forming an enzyme-substrate complex.
  • The active site is a pocket within the enzyme's tertiary and quaternary structure.
  • The Lock and Key and Induced-fit theories explain enzyme specificity.
  • Enzyme names usually end in "-ase" and indicate their function.
  • Enzymes are classified using EC numbers, divided into six main classes based on reaction type.
  • Oxidoreductases (EC 1) catalyze oxidation/reduction reactions
  • Transferases (EC 2) catalyze the transfer of chemical groups
  • Hydrolases (EC 3) catalyze the hydrolysis of chemical bonds
  • Lyases (EC 4) catalyze the cleavage of chemical bonds without oxidation or hydrolysis
  • Isomerases (EC 5) catalyze geometric and structural changes between isomers
  • Ligases (EC 6) catalyze the joining of two compounds with ATP hydrolysis
  • Translocases (EC 7) catalyze the transport of substances across membranes, added in 2018
  • EC numbers have four digits, indicating enzyme class, subclass, sub-subclass, and serial number.
  • Enzymes are excellent catalysts, accelerating reactions significantly.
  • Enzyme activity is regulated by temperature, pH, and additives.
  • Enzymes reduce activation energy by altering the reaction's transition state.
  • Enzyme activity is significantly influenced by pH and temperature.
  • Enzymes function optimally at specific pH and temperature levels.
  • Enzyme activity can be affected by inhibitors (decrease activity) or activators (increase activity).
  • Many drugs and poisons act as enzyme inhibitors.
  • Enzyme activity can be modulated through inhibition.
  • Reversible inhibitors bind non-covalently and can be reversed as there is no interaction between inhibitor and substrate
  • Irreversible inhibitors bind via covalent bonds, preventing enzyme activity and are irreversible because of strong covalent bonding
  • Competitive inhibitors bind to the active site, while non-competitive inhibitors bind elsewhere and alter the enzyme's shape, which reduce activity.
  • Enzymes can be activated by ions, cofactors, coenzymes, or conversion of a proenzyme into an active molecule.
  • Activators bind to enzymes and enhance their metabolic activity.

Cofactors and Coenzymes: Enzyme Assistants

  • Some enzymes need cofactors or coenzymes to function.
  • Cofactors are inorganic ions or organic molecules that assist enzymes.
  • Coenzymes are organic molecules, often vitamin-derived, that function as cofactors.
  • Metalloproteins are enzymes with tightly bound metal ions at the active sites.
  • Examples of metalloenzymes contain iron, zinc, copper, or cobalt.
  • Water-soluble vitamins are precursors to coenzymes.
  • B vitamins (Thiamin, Riboflavin, Niacin, Pantothenic Acid, Pyridoxine, Biotin, Folic Acid, Cobalamin) and Vitamin C are water soluble-vitamins.
  • Thiamin (Vitamin B1) is part of thiamin pyrophosphate (TPP) and participates in decarboxylation.
  • Riboflavin (Vitamin B2) forms flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), which helps with redox reactions.
  • Niacin (Vitamin B3) is part of nicotinamide adenine dinucleotide (NAD+) and NADP+ and participates in redox reactions.
  • Pantothenic Acid (Vitamin B5) is part of coenzyme A (CoA) and participates in energy production and lipid/amino acid metabolism.
  • Pyridoxine (Vitamin B6) is converted to pyridoxal phosphate (PLP) and participates in amino acid transamination and decarboxylation.
  • Biotin participates in carboxyl-group transfer reactions.
  • Folic Acid (B9) forms tetrahydrofolate (THFA) for help with nucleic acid synthesis.
  • Cobalamin (Vitamin B12) participates in methyl group transfer.
  • Vitamin C (Ascorbic Acid) is an antioxidant and participates in collagen synthesis and biogenic amine biosynthesis

Heterocyclic Compounds: Cyclic Structures with Heteroatoms

  • Heterocyclic compounds are organic compounds where one or more carbon atoms in a ring are replaced by heteroatoms
  • Common heteroatoms include oxygen, nitrogen, or sulfur.
  • Heterocycles are the largest class of organic compounds, found in natural products and drugs.
  • Classification is based on the number of atoms in the ring.
  • Classification is also based on the type of heteroatoms and the number of rings (monocyclic or polycyclic).
  • Pyrrole derivatives (porphyrins) form building blocks of biologically important compounds.
  • Heme, an iron-porphyrin complex, is responsible for the red color of arterial blood and is found in hemoglobin.
  • Indole is a fused-ring system found in tryptophan and its derivatives like serotonin.
  • Pyrimidines such as Cytosine, Thymine, and Uracil are bases found in nucleic acids.
  • Purines such as Adenine and Guanine are bases found in nucleic acids.

Nucleosides, Nucleotides, and Nucleic Acids: Building Blocks of Genetic Material

  • Nucleosides consist of a nitrogenous base linked to a sugar (ribose or deoxyribose) via a glycosidic bond.
  • Nucleotides are 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) are polymers of nucleotides linked by phosphodiester bonds that store information for cellular growth and reproduction.

DNA (Deoxyribonucleic Acid): The Genetic Code

  • DNA has a double-stranded helix structure and contains deoxyribose sugar.
  • The bases in DNA are Adenine (A), Guanine (G), Cytosine (C), and Thymine (T).
  • Base pairing in DNA follows the rule: A-T, G-C, connected by hydrogen bonds.
  • DNA primary structure features alternating 2-deoxy-ribose and phosphate units in the backbone.

RNA (Ribonucleic Acid): Genetic Messenger & More

  • RNA is generally single-stranded and contains ribose sugar.
  • The bases in RNA are Adenine (A), Guanine (G), Cytosine (C), and Uracil (U).
  • RNA functions as mRNA (messenger), rRNA (ribosomal), and tRNA (transfer).

Key Differences Between DNA and RNA

  • RNA consists of a single strand and is shorter, while DNA is double-stranded and longer.
  • DNA nucleotides contain Deoxyribose, a phosphate group, and one of four nitrogenous bases like Adenine, Guanine, Thymine, or Cytosine.
  • RNA nucleotides contain Ribose, a phosphate group, and one of four nitrogenous bases such as Adenine, Guanine, Uracil, or Cytosine.

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