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Questions and Answers
Enzymes are consumed during reactions, leading to alterations in their structure and function.
Enzymes are consumed during reactions, leading to alterations in their structure and function.
False (B)
Enzyme specificity arises solely from the charge distribution on the enzyme surface.
Enzyme specificity arises solely from the charge distribution on the enzyme surface.
False (B)
Enzymes bind substrates at a general location on the enzyme's surface.
Enzymes bind substrates at a general location on the enzyme's surface.
False (B)
The 'Lock and Key Theory' suggests that enzymes undergo a conformational change to accommodate the substrate.
The 'Lock and Key Theory' suggests that enzymes undergo a conformational change to accommodate the substrate.
Enzymes are systematically identified with an EC number, classifying them into eight main classes.
Enzymes are systematically identified with an EC number, classifying them into eight main classes.
Lyases catalyze reactions involving the cleavage of chemical bonds through oxidation or hydrolysis.
Lyases catalyze reactions involving the cleavage of chemical bonds through oxidation or hydrolysis.
The first number of the EC number indicates the sub-subclass of the enzyme.
The first number of the EC number indicates the sub-subclass of the enzyme.
Enzyme activity is solely regulated by temperature and pH levels.
Enzyme activity is solely regulated by temperature and pH levels.
Enzymes primarily lower the activation energy required for a reaction by increasing the kinetic energy of the reacting molecules.
Enzymes primarily lower the activation energy required for a reaction by increasing the kinetic energy of the reacting molecules.
Enzyme activity is consistently optimal across a broad range of pH and temperature values.
Enzyme activity is consistently optimal across a broad range of pH and temperature values.
Inhibitors enhance enzyme activity, while activators decrease enzyme activity.
Inhibitors enhance enzyme activity, while activators decrease enzyme activity.
Reversible inhibition involves the formation of covalent bonds between the inhibitor and the enzyme.
Reversible inhibition involves the formation of covalent bonds between the inhibitor and the enzyme.
Irreversible inhibitors can be readily displaced from the enzyme active site by increasing substrate concentration.
Irreversible inhibitors can be readily displaced from the enzyme active site by increasing substrate concentration.
Non-competitive inhibitors bind to the active site, preventing the substrate from binding.
Non-competitive inhibitors bind to the active site, preventing the substrate from binding.
Non-competitive inhibitors do not alter the shape of the enzyme.
Non-competitive inhibitors do not alter the shape of the enzyme.
Enzyme activation always involves the binding of a coenzyme.
Enzyme activation always involves the binding of a coenzyme.
Cofactors are organic molecules that assist enzymes.
Cofactors are organic molecules that assist enzymes.
Coenzymes are inorganic ions that function as enzyme helpers.
Coenzymes are inorganic ions that function as enzyme helpers.
Metalloproteins contain loosely attached metal ions at their active sites.
Metalloproteins contain loosely attached metal ions at their active sites.
Water-soluble vitamins directly act as enzymes in biochemical reactions.
Water-soluble vitamins directly act as enzymes in biochemical reactions.
Thiamin (Vitamin B1) is involved in oxidation and reduction reactions.
Thiamin (Vitamin B1) is involved in oxidation and reduction reactions.
Riboflavin (Vitamin B2) forms nicotinamide adenine dinucleotide (NAD+).
Riboflavin (Vitamin B2) forms nicotinamide adenine dinucleotide (NAD+).
Niacin (Vitamin B3) is not involved in redox reactions.
Niacin (Vitamin B3) is not involved in redox reactions.
Pantothenic Acid (Vitamin B5) is involved in nucleic acid synthesis.
Pantothenic Acid (Vitamin B5) is involved in nucleic acid synthesis.
Pyridoxine (Vitamin B6) is converted to tetrahydrofolate (THFA).
Pyridoxine (Vitamin B6) is converted to tetrahydrofolate (THFA).
Biotin is involved in methyl-group transfer reactions.
Biotin is involved in methyl-group transfer reactions.
Folic Acid (B9) forms pyridoxal phosphate (PLP).
Folic Acid (B9) forms pyridoxal phosphate (PLP).
Cobalamin (Vitamin B12) is involved in carboxyl-group transfer reactions.
Cobalamin (Vitamin B12) is involved in carboxyl-group transfer reactions.
Vitamin C (Ascorbic Acid) solely acts as a pro-oxidant in biological systems.
Vitamin C (Ascorbic Acid) solely acts as a pro-oxidant in biological systems.
Heterocyclic compounds contain only carbon and hydrogen atoms in their ring structures.
Heterocyclic compounds contain only carbon and hydrogen atoms in their ring structures.
Heterocycles form a small class of organic compounds.
Heterocycles form a small class of organic compounds.
Porphyrins are not pyrrole derivatives.
Porphyrins are not pyrrole derivatives.
Heme is not responsible for the red color of aterial blood.
Heme is not responsible for the red color of aterial blood.
Indole is a saturated ring system found in alanine.
Indole is a saturated ring system found in alanine.
Uracil is exclusively found in DNA.
Uracil is exclusively found in DNA.
Adenine is not found in nucleic acids.
Adenine is not found in nucleic acids.
Nucleosides contain phosphate groups.
Nucleosides contain phosphate groups.
Nucleotides are solely structural components of DNA and RNA, lacking other cellular functions.
Nucleotides are solely structural components of DNA and RNA, lacking other cellular functions.
In DNA, adenine pairs with cytosine and guanine pairs with thymine.
In DNA, adenine pairs with cytosine and guanine pairs with thymine.
RNA predominantly exists as a double-stranded helix, similar to DNA.
RNA predominantly exists as a double-stranded helix, similar to DNA.
Enzymes accelerate reaction rates by increasing the activation energy required for a reaction to proceed.
Enzymes accelerate reaction rates by increasing the activation energy required for a reaction to proceed.
In competitive inhibition, inhibitors bind to a site other than the active site, altering the enzyme's shape and reducing its activity.
In competitive inhibition, inhibitors bind to a site other than the active site, altering the enzyme's shape and reducing its activity.
Metalloproteins are enzymes that contain loosely bound metal ions at their active sites, facilitating catalytic activity.
Metalloproteins are enzymes that contain loosely bound metal ions at their active sites, facilitating catalytic activity.
In DNA, adenine always pairs with uracil, while guanine always pairs with cytosine.
In DNA, adenine always pairs with uracil, while guanine always pairs with cytosine.
Translocases are classified under EC 8, catalyzing the transfer of substances across cellular membranes.
Translocases are classified under EC 8, catalyzing the transfer of substances across cellular membranes.
Flashcards
Enzymes Role and Function
Enzymes Role and Function
Biological catalysts accelerating reaction rates in living cells, mediating metabolism.
Enzymes Specificity
Enzymes Specificity
Enzymes are substrate-specific catalysts enhancing reaction rates without being used up in the process.
Active Site
Active Site
Region on an enzyme where substrates bind, forming an enzyme-substrate complex.
Enzyme Nomenclature
Enzyme Nomenclature
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Oxidoreductases (EC 1)
Oxidoreductases (EC 1)
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Transferases (EC 2)
Transferases (EC 2)
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Hydrolases (EC 3)
Hydrolases (EC 3)
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Lyases (EC 4)
Lyases (EC 4)
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Isomerases (EC 5)
Isomerases (EC 5)
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Ligases (EC 6)
Ligases (EC 6)
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Translocases (EC 7)
Translocases (EC 7)
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Enzyme activity regulators
Enzyme activity regulators
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Enzymes action
Enzymes action
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Definition of Inhibitors
Definition of 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 inhibitors
Non-competitive 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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Heterocyclic Compounds
Heterocyclic Compounds
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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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Nucleotide Function
Nucleotide Function
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DNA (Deoxyribonucleic Acid)
DNA (Deoxyribonucleic Acid)
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RNA (Ribonucleic Acid)
RNA (Ribonucleic Acid)
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DNA Bases
DNA Bases
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RNA Bases
RNA Bases
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Study Notes
Enzymes: Biological Catalysts
- Enzymes act as biological catalysts, accelerating reaction rates within living cells.
- Enzymes are critical for metabolism and life processes within cells.
- Enzymes exhibit specificity, enhancing reaction rates without being consumed.
- Specificity results from complementary shapes, charges, and characteristics between the enzyme and its substrates.
Enzyme-Substrate Interaction
- Enzymes bind substrates at the active site to form an enzyme-substrate complex.
- The active site is a pocket formed by the enzyme's tertiary and quaternary structure.
- Specificity is explained by the "Lock and Key" and "Induced-fit" theories.
Enzyme Classification
- Enzyme names usually indicate their function with the suffix "-ase".
- Enzymes are classified using an EC (Enzyme Commission) number into main classes based on reaction type.
- EC 1: Oxidoreductases catalyze oxidation/reduction reactions.
- EC 2: Transferases transfer chemical groups.
- EC 3: Hydrolases catalyze the hydrolysis of chemical bonds.
- EC 4: Lyases catalyze the cleavage of chemical bonds (excluding oxidation or hydrolysis).
- EC 5: Isomerases catalyze geometric and structural changes between isomers.
- EC 6: Ligases join two compounds utilizing ATP hydrolysis.
- EC 7: Translocases transport substances across membranes (added in 2018).
- The EC number has four digits indicating class, subclass, sub-subclass, and serial number.
Enzyme Properties and Regulation
- Enzymes are excellent catalysts, accelerating reactions significantly.
- Activity is regulated by temperature, pH, and additives.
- Enzymes lower activation energy by forcing molecules through a different transition state.
- Activity is affected by pH and temperature, with enzymes functioning best at specific levels.
- Enzyme activity can be affected by inhibitors, which decrease activity, and activators, which increase activity.
Enzyme Inhibition
- Enzyme activity can be modulated by inhibitors.
- Reversible inhibition involves non-covalent binding, without any chemical changes, and is reversible.
- Irreversible inhibition involves covalent bond, preventing catalytic activity, and is irreversible.
- Competitive inhibitors bind to the active site.
- Non-competitive inhibitors bind elsewhere and alter the enzyme's shape.
Enzyme Activation
- Enzymes are activated by ions (Ca2+, Mg2+), cofactors, coenzymes, or proenzyme conversion.
- Enzyme activation converts an inactive enzyme molecule into a metabolically active form.
- Activators bind to enzyme molecules and boost their metabolic activity.
Cofactors and Coenzymes
- Some enzymes need cofactors or coenzymes to function.
- Cofactors are inorganic ions or organic molecules that assist enzymes.
- Coenzymes are organic molecules that function as cofactors, often derived from vitamins.
- Metalloproteins are enzymes containing tightly bound metal ions at their active sites.
Water-Soluble Vitamins as Coenzyme Precursors
- Water-soluble vitamins are precursors to coenzymes.
- B vitamins (Thiamin, Riboflavin, Niacin, Pantothenic Acid, Pyridoxine, Biotin, Folic Acid, Cobalamin) and Vitamin C are included.
- Thiamin (Vitamin B1) is part of thiamin pyrophosphate (TPP) and is involved in decarboxylation.
- Riboflavin (Vitamin B2) constitutes flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), for redox reactions.
- Niacin (Vitamin B3) is part of nicotinamide adenine dinucleotide (NAD+) and NADP+, for redox reactions.
- Pantothenic Acid (Vitamin B5) is part of coenzyme A (CoA), involved in energy production and lipid/amino acid metabolism.
- Pyridoxine (Vitamin B6) is converted to pyridoxal phosphate (PLP), involved in amino acid transamination and decarboxylation.
- Biotin is involved in carboxyl-group transfer reactions.
- Folic Acid (B9) constitutes tetrahydrofolate (THFA), for nucleic acid synthesis.
- Cobalamin (Vitamin B12) is involved in methyl group transfer.
- Vitamin C (Ascorbic Acid) acts as an antioxidant and participates in collagen synthesis and biogenic amine biosynthesis.
Heterocyclic Compounds
- Heterocyclic compounds are organic with one or more carbon atoms replaced by heteroatoms in a ring structure.
- They are classified by the number of atoms in the ring, type of heteroatoms, and number of rings.
- Pyrrole derivatives (Porphyrins) are building blocks of compounds that are biologically important.
- 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 in tryptophan and serotonin derivatives.
- Pyrimidines (Cytosine, Thymine, Uracil) and Purines (Adenine, Guanine) are bases found in nucleic acids.
Nucleosides and Nucleotides
- 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 are building blocks for DNA and RNA, sources of energy (ATP), second messengers, and intracellular signaling switches.
Nucleic Acids: DNA and RNA
- Nucleic acids (DNA and RNA) are polymers of nucleotides linked by phosphodiester bonds.
- Important molecules store information that is crucial for cellular growth and reproduction.
- Two types of nucleic acids: deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).
DNA
- DNA (Deoxyribonucleic Acid) has a double-stranded helix.
- Contains deoxyribose sugar, and the bases are Adenine (A), Guanine (G), Cytosine (C), Thymine (T).
- Base pairing follows A-T and G-C.
- Primary structure includes alternating 2-deoxy-ribose and phosphate units in the backbone.
RNA
- RNA (Ribonucleic Acid) is single-stranded and contains ribose sugar.
- Bases: Adenine (A), Guanine (G), Cytosine (C), Uracil (U).
- mRNA (messenger), rRNA (ribosomal), and tRNA (transfer) are included in functions.
Key Differences Between DNA and RNA
- RNA is single-stranded and shorter, while DNA is double-stranded and very long.
- DNA nucleotides contain Deoxyribose, Phosphate, and one of four nitrogenous bases (Adenine, Guanine, Thymine, Cytosine).
- RNA nucleotides contain Ribose, Phosphate, and one of four nitrogenous bases (Adenine, Guanine, Uracil, Cytosine).
Conclusion
- Enzymes, cofactors, heterocyclic compounds, nucleotides, and nucleic acids are vital components of life.
- Grasping structure, function, and interactions is essential to understand biological processes.
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