Podcast
Questions and Answers
What characteristic of enzymes is most directly responsible for their ability to catalyze specific reactions?
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?
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?
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?
What type of enzyme inhibition involves the inhibitor binding to a site other than the active site, thus altering enzyme conformation?
Which of the following is NOT a common method of enzyme activation?
Which of the following is NOT a common method of enzyme activation?
Which of the following best describes the role of coenzymes?
Which of the following best describes the role of coenzymes?
Which vitamin is a precursor to coenzyme A (CoA), vital for energy production and lipid/amino acid metabolism?
Which vitamin is a precursor to coenzyme A (CoA), vital for energy production and lipid/amino acid metabolism?
What is a key structural feature of heterocyclic compounds?
What is a key structural feature of heterocyclic compounds?
What is the role of the iron-porphyrin complex known as heme?
What is the role of the iron-porphyrin complex known as heme?
Which of the following is a key difference between a nucleoside and a nucleotide?
Which of the following is a key difference between a nucleoside and a nucleotide?
In DNA, which of the following base pairings is correct?
In DNA, which of the following base pairings is correct?
What is the primary structural difference between RNA and DNA?
What is the primary structural difference between RNA and DNA?
What role do transferases (EC 2) play in enzymatic reactions?
What role do transferases (EC 2) play in enzymatic reactions?
According to the 'lock and key' theory of enzyme specificity, what is the relationship between an enzyme and its substrate?
According to the 'lock and key' theory of enzyme specificity, what is the relationship between an enzyme and its substrate?
If an enzyme's activity is most efficient at a specific pH, what would happen if the pH is drastically altered?
If an enzyme's activity is most efficient at a specific pH, what would happen if the pH is drastically altered?
Which type of inhibition involves the inhibitor permanently binding to the enzyme, often through covalent bonds?
Which type of inhibition involves the inhibitor permanently binding to the enzyme, often through covalent bonds?
What is the main function of ligases (EC 6) in biochemical reactions?
What is the main function of ligases (EC 6) in biochemical reactions?
How do competitive inhibitors affect enzyme activity when substrate concentration increases?
How do competitive inhibitors affect enzyme activity when substrate concentration increases?
What is the role of metalloproteins in enzyme function?
What is the role of metalloproteins in enzyme function?
Which water-soluble vitamin is a component of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN)?
Which water-soluble vitamin is a component of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN)?
What is the role of Vitamin C (Ascorbic Acid) in biological systems?
What is the role of Vitamin C (Ascorbic Acid) in biological systems?
What characteristic defines lyases (EC 4) as a distinct class of enzymes?
What characteristic defines lyases (EC 4) as a distinct class of enzymes?
How do translocases (EC 7) facilitate biological processes?
How do translocases (EC 7) facilitate biological processes?
In the context of enzyme regulation, what is the role of an activator?
In the context of enzyme regulation, what is the role of an activator?
Which of the following vitamins is essential for carboxylation reactions?
Which of the following vitamins is essential for carboxylation reactions?
Which of the following best describes the structure of DNA?
Which of the following best describes the structure of DNA?
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?
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?
Which function is associated with nucleic acids (DNA and RNA)?
Which function is associated with nucleic acids (DNA and RNA)?
What is the effect of a non-competitive inhibitor on the enzyme's activity?
What is the effect of a non-competitive inhibitor on the enzyme's activity?
Which class of enzymes catalyzes the joining of two large molecules by forming a new chemical bond, often with accompanying ATP hydrolysis?
Which class of enzymes catalyzes the joining of two large molecules by forming a new chemical bond, often with accompanying ATP hydrolysis?
Which of the following is a characteristic feature of transfer RNA (tRNA)?
Which of the following is a characteristic feature of transfer RNA (tRNA)?
What role does pyridoxal phosphate (PLP), derived from Pyridoxine (Vitamin B6) play in metabolic processes?
What role does pyridoxal phosphate (PLP), derived from Pyridoxine (Vitamin B6) play in metabolic processes?
If an enzyme is described as having substrate specificity, what does this signify?
If an enzyme is described as having substrate specificity, what does this signify?
Which of the following describes the function of isomerases (EC 5)?
Which of the following describes the function of isomerases (EC 5)?
Which of the following best describes why understanding enzymes, cofactors, heterocyclic compounds, nucleotides, and nucleic acids are essential?
Which of the following best describes why understanding enzymes, cofactors, heterocyclic compounds, nucleotides, and nucleic acids are essential?
Which compound does NOT represent a base incorporated into the structure of RNA?
Which compound does NOT represent a base incorporated into the structure of RNA?
How does the induced-fit theory refine the 'lock and key' model of enzyme-substrate interaction?
How does the induced-fit theory refine the 'lock and key' model of enzyme-substrate interaction?
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?
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?
How do metalloenzymes utilize metal ions in their catalytic mechanisms?
How do metalloenzymes utilize metal ions in their catalytic mechanisms?
How do water-soluble vitamins function as precursors to coenzymes?
How do water-soluble vitamins function as precursors to coenzymes?
How do nucleic acids, such as DNA and RNA, store and transmit genetic information?
How do nucleic acids, such as DNA and RNA, store and transmit genetic information?
Flashcards
Enzymes
Enzymes
Biological catalysts accelerating reaction rates in living cells.
Enzyme Specificity
Enzyme Specificity
Enzymes are specific to the substrates they bind to.
Active Site
Active Site
Region of an enzyme where substrates bind to facilitate a reaction.
EC Number
EC Number
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Inhibitors
Inhibitors
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Reversible inhibition
Reversible inhibition
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Irreversible inhibition
Irreversible inhibition
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Competitive Inhibitors
Competitive Inhibitors
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Non-competitive reversible inhibitors
Non-competitive reversible inhibitors
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Activation
Activation
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Cofactors/Coenzymes
Cofactors/Coenzymes
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Cofactors
Cofactors
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Coenzymes
Coenzymes
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Metalloproteins
Metalloproteins
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Water-Soluble Vitamins
Water-Soluble Vitamins
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Thiamin (Vitamin B1)
Thiamin (Vitamin B1)
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Riboflavin (Vitamin B2)
Riboflavin (Vitamin B2)
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Niacin (Vitamin B3)
Niacin (Vitamin B3)
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Pantothenic Acid (Vitamin B5)
Pantothenic Acid (Vitamin B5)
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Pyridoxine (Vitamin B6)
Pyridoxine (Vitamin B6)
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Biotin
Biotin
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Folic Acid (B9)
Folic Acid (B9)
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Cobalamin (Vitamin B12)
Cobalamin (Vitamin B12)
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Vitamin C (Ascorbic Acid)
Vitamin C (Ascorbic Acid)
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Heterocyclic Compounds
Heterocyclic Compounds
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Porphyrins
Porphyrins
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Heme
Heme
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Indole
Indole
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Pyrimidines
Pyrimidines
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Purines
Purines
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Nucleosides
Nucleosides
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Nucleotide Function
Nucleotide Function
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Nucleic Acids
Nucleic Acids
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DNA
DNA
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RNA
RNA
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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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