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Questions and Answers
Which statement best describes the role of enzymes in biochemical reactions?
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?
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?
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?
An enzyme is classified as EC 3.2.1.1. What type of reaction does this enzyme catalyze?
How do enzymes enhance reaction rates?
How do enzymes enhance reaction rates?
Why do changes in pH and temperature affect enzyme activity?
Why do changes in pH and temperature affect enzyme activity?
Which of the following describes a reversible enzyme inhibitor?
Which of the following describes a reversible enzyme inhibitor?
How do competitive enzyme inhibitors affect enzyme activity?
How do competitive enzyme inhibitors affect enzyme activity?
How do non-competitive inhibitors affect enzyme activity?
How do non-competitive inhibitors affect enzyme activity?
Which of the following is an example of enzyme activation?
Which of the following is an example of enzyme activation?
What is the general role of cofactors and coenzymes in enzyme function?
What is the general role of cofactors and coenzymes in enzyme function?
Which of the following is an example of a cofactor?
Which of the following is an example of a cofactor?
What is the primary difference between a cofactor and a coenzyme?
What is the primary difference between a cofactor and a coenzyme?
What is the role of metalloproteins in enzyme catalysis?
What is the role of metalloproteins in enzyme catalysis?
If a patient is deficient in thiamin (Vitamin B1), which enzymatic reaction might be impaired?
If a patient is deficient in thiamin (Vitamin B1), which enzymatic reaction might be impaired?
Which vitamin is essential for the formation of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN)?
Which vitamin is essential for the formation of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN)?
Niacin (Vitamin B3) plays a critical role in which type of biochemical reactions?
Niacin (Vitamin B3) plays a critical role in which type of biochemical reactions?
Pantothenic acid is a component of which coenzyme?
Pantothenic acid is a component of which coenzyme?
Pyridoxine (Vitamin B6) is important for which type of biochemical reaction?
Pyridoxine (Vitamin B6) is important for which type of biochemical reaction?
Cobalamin (Vitamin B12) is directly involved in which metabolic process?
Cobalamin (Vitamin B12) is directly involved in which metabolic process?
Vitamin C (Ascorbic Acid) acts as an antioxidant with what addition role in the body?
Vitamin C (Ascorbic Acid) acts as an antioxidant with what addition role in the body?
What is a general characteristic of heterocyclic compounds?
What is a general characteristic of heterocyclic compounds?
What is the main function of porphyrins in biological systems?
What is the main function of porphyrins in biological systems?
What is the role of heme in the body?
What is the role of heme in the body?
Which of the following molecules is a derivative of indole?
Which of the following molecules is a derivative of indole?
What is the major structural difference between purines and pyrimidines?
What is the major structural difference between purines and pyrimidines?
Which of the following best describes a nucleoside?
Which of the following best describes a nucleoside?
What distinguishes a nucleotide from a nucleoside?
What distinguishes a nucleotide from a nucleoside?
What are the primary functions of nucleotides in cells?
What are the primary functions of nucleotides in cells?
What type of bond links nucleotides together to form nucleic acids?
What type of bond links nucleotides together to form nucleic acids?
Which nitrogenous base is unique to DNA?
Which nitrogenous base is unique to DNA?
What is the base pairing rule in DNA?
What is the base pairing rule in DNA?
How does the sugar component differ between DNA and RNA?
How does the sugar component differ between DNA and RNA?
What is the key structural difference between DNA and RNA molecules?
What is the key structural difference between DNA and RNA molecules?
Which of the following is a function of mRNA?
Which of the following is a function of mRNA?
Which of the following molecules correctly illustrates the key differences between DNA and RNA nucleotides:
Which of the following molecules correctly illustrates the key differences between DNA and RNA nucleotides:
Which of the following best explains why enzymes exhibit high specificity for their substrates?
Which of the following best explains why enzymes exhibit high specificity for their substrates?
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?
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?
How do irreversible enzyme inhibitors differ fundamentally from reversible inhibitors in their mechanism of action?
How do irreversible enzyme inhibitors differ fundamentally from reversible inhibitors in their mechanism of action?
Which of the following best describes the role of a coenzyme in an enzymatic reaction?
Which of the following best describes the role of a coenzyme in an enzymatic reaction?
How does Vitamin B1 (Thiamin) contribute to enzyme function?
How does Vitamin B1 (Thiamin) contribute to enzyme function?
Flashcards
Enzymes
Enzymes
Biological catalysts that accelerate reaction rates within living cells.
Enzyme Specificity
Enzyme Specificity
The characteristic of enzymes being selective in the reactions they catalyze.
Enzyme Active Site
Enzyme Active Site
A specific region on an enzyme where substrates bind.
Enzyme Names
Enzyme Names
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EC Number
EC Number
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Enzyme Catalysis
Enzyme Catalysis
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Enzyme Inhibitors
Enzyme Inhibitors
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Reversible Inhibition
Reversible Inhibition
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Irreversible Inhibition
Irreversible Inhibition
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Enzyme Activators
Enzyme Activators
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Cofactors and Coenzymes
Cofactors and 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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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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Heterocyclic Classification (Number of Atoms)
Heterocyclic Classification (Number of Atoms)
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Pyrrole Derivatives (Porphyrins)
Pyrrole Derivatives (Porphyrins)
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Heme
Heme
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Nucleosides
Nucleosides
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Nucleotides
Nucleotides
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Nucleic Acids (DNA and RNA)
Nucleic Acids (DNA and RNA)
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DNA (Deoxyribonucleic Acid)
DNA (Deoxyribonucleic Acid)
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RNA (Ribonucleic Acid)
RNA (Ribonucleic Acid)
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Bases in DNA
Bases in DNA
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Bases in RNA
Bases in RNA
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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.
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