Enzymes: Biological Catalysts

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Questions and Answers

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.

False (B)

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.

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

Enzymes are systematically identified with an EC number, classifying them into eight main classes.

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

Lyases catalyze reactions involving the cleavage of chemical bonds through oxidation or hydrolysis.

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

The first number of the EC number indicates the sub-subclass of the enzyme.

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

Enzyme activity is solely regulated by temperature and pH levels.

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

Enzymes primarily lower the activation energy required for a reaction by increasing the kinetic energy of the reacting molecules.

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

Enzyme activity is consistently optimal across a broad range of pH and temperature values.

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

Inhibitors enhance enzyme activity, while activators decrease enzyme activity.

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

Reversible inhibition involves the formation of covalent bonds between the inhibitor and the enzyme.

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

Irreversible inhibitors can be readily displaced from the enzyme active site by increasing substrate concentration.

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

Non-competitive inhibitors bind to the active site, preventing the substrate from binding.

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

Non-competitive inhibitors do not alter the shape of the enzyme.

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

Enzyme activation always involves the binding of a coenzyme.

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

Cofactors are organic molecules that assist enzymes.

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

Coenzymes are inorganic ions that function as enzyme helpers.

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

Metalloproteins contain loosely attached metal ions at their active sites.

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

Water-soluble vitamins directly act as enzymes in biochemical reactions.

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

Thiamin (Vitamin B1) is involved in oxidation and reduction reactions.

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

Riboflavin (Vitamin B2) forms nicotinamide adenine dinucleotide (NAD+).

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

Niacin (Vitamin B3) is not involved in redox reactions.

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

Pantothenic Acid (Vitamin B5) is involved in nucleic acid synthesis.

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

Pyridoxine (Vitamin B6) is converted to tetrahydrofolate (THFA).

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

Biotin is involved in methyl-group transfer reactions.

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

Folic Acid (B9) forms pyridoxal phosphate (PLP).

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

Cobalamin (Vitamin B12) is involved in carboxyl-group transfer reactions.

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

Vitamin C (Ascorbic Acid) solely acts as a pro-oxidant in biological systems.

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

Heterocyclic compounds contain only carbon and hydrogen atoms in their ring structures.

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

Heterocycles form a small class of organic compounds.

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

Porphyrins are not pyrrole derivatives.

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

Heme is not responsible for the red color of aterial blood.

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

Indole is a saturated ring system found in alanine.

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

Uracil is exclusively found in DNA.

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

Adenine is not found in nucleic acids.

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

Nucleosides contain phosphate groups.

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

Nucleotides are solely structural components of DNA and RNA, lacking other cellular functions.

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

In DNA, adenine pairs with cytosine and guanine pairs with thymine.

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

RNA predominantly exists as a double-stranded helix, similar to DNA.

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

Enzymes accelerate reaction rates by increasing the activation energy required for a reaction to proceed.

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

In competitive inhibition, inhibitors bind to a site other than the active site, altering the enzyme's shape and reducing its activity.

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

Metalloproteins are enzymes that contain loosely bound metal ions at their active sites, facilitating catalytic activity.

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

In DNA, adenine always pairs with uracil, while guanine always pairs with cytosine.

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

Translocases are classified under EC 8, catalyzing the transfer of substances across cellular membranes.

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

Flashcards

Enzymes Role and Function

Biological catalysts accelerating reaction rates in living cells, mediating metabolism.

Enzymes Specificity

Enzymes are substrate-specific catalysts enhancing reaction rates without being used up in the process.

Active Site

Region on an enzyme where substrates bind, forming an enzyme-substrate complex.

Enzyme Nomenclature

Enzyme names indicate function with "-ase" suffix; classified by EC number based on reaction type.

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Oxidoreductases (EC 1)

Oxidation/reduction reactions.

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Transferases (EC 2)

Transfer of chemical groups.

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Hydrolases (EC 3)

Hydrolysis of chemical bonds.

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Lyases (EC 4)

Cleavage of chemical bonds (not by oxidation or hydrolysis).

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Isomerases (EC 5)

Geometric and structural changes between isomers.

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Ligases (EC 6)

Joining two compounds with ATP hydrolysis.

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Translocases (EC 7)

Transport of substances across membranes.

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Enzyme activity regulators

Temperature, pH and additives.

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Enzymes action

Lower the activation energy required for a reaction.

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Definition of Inhibitors

Molecules that decrease enzyme activity.

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Reversible inhibition

Binds via non covalent interaction. Do not perform any chemical changes

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Irreversible inhibition

Binds via covalent bond.

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Competitive inhibitors

Bind to the active site of an enzyme, preventing the substrate from binding.

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Non-competitive inhibitors

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

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Activation

The process of converting an inactive enzyme molecule into a metabolically active molecule.

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Cofactors/Coenzymes

Additional molecules required by some enzymes to function.

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Cofactors

Inorganic ions or organic molecules that assist enzymes.

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Coenzymes

Organic molecules that function as cofactors, often derived from vitamins.

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Metalloproteins

Enzymes containing tightly bound metal ions at their active sites.

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Water-Soluble Vitamins

Many water-soluble vitamins are precursors to coenzymes.

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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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Heterocyclic Compounds

Organic compounds with heteroatoms in a ring structure.

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Pyrrole derivatives (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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Nucleosides

A nitrogenous base linked to a sugar via a glycosidic bond.

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Nucleotide Function

Building blocks for DNA and RNA, Intracellular source of energy (ATP), Second messengers, Intracellular signalling switches.

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DNA (Deoxyribonucleic Acid)

Double-stranded helix. Contains deoxyribose sugar.

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RNA (Ribonucleic Acid)

Single-stranded. Contains ribose sugar.

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DNA Bases

Adenine, guanine, cytosine, and thymine.

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RNA Bases

Adenine, guanine, cytosine, and uracil.

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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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