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Questions and Answers
What type of compounds are found in living organisms?
What type of compounds are found in living organisms?
organic compounds
Which elements are found in both non-living matter and living tissues?
Which elements are found in both non-living matter and living tissues?
All elements present in a sample of earth’s crust are also present in a sample of living tissue.
All elements present in a sample of earth’s crust are also present in a sample of living tissue.
True
___________ compounds are generally water insoluble.
___________ compounds are generally water insoluble.
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Match the following organic compounds with their classification:
Match the following organic compounds with their classification:
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What is the tertiary structure of a protein?
What is the tertiary structure of a protein?
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What is the quaternary structure of a protein?
What is the quaternary structure of a protein?
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What type of molecules are almost all enzymes?
What type of molecules are almost all enzymes?
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Enzymes isolated from thermophilic organisms are stable at high temperatures.
Enzymes isolated from thermophilic organisms are stable at high temperatures.
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What are compounds other than primary metabolites called?
What are compounds other than primary metabolites called?
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What is the most abundant chemical in living organisms?
What is the most abundant chemical in living organisms?
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Lipids are strictly considered macromolecules.
Lipids are strictly considered macromolecules.
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Proteins are linear chains of __________ linked by peptide bonds.
Proteins are linear chains of __________ linked by peptide bonds.
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Match the following nucleotide components:
Match the following nucleotide components:
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What is the term for the temperature and pH at which an enzyme shows its highest activity?
What is the term for the temperature and pH at which an enzyme shows its highest activity?
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What is the term used for the maximum velocity of an enzymatic reaction?
What is the term used for the maximum velocity of an enzymatic reaction?
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What is the term for inhibition where the inhibitor closely resembles the substrate and competes for the substrate-binding site?
What is the term for inhibition where the inhibitor closely resembles the substrate and competes for the substrate-binding site?
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Enzymes are composed of one or several ______ chains.
Enzymes are composed of one or several ______ chains.
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Match the enzyme classification with the type of reactions they catalyze:
Match the enzyme classification with the type of reactions they catalyze:
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Study Notes
Biomolecules
- Biomolecules are chemical compounds found in living organisms.
- They can be classified into two categories: micromolecules (biomolecules) and macromolecules (biomacromolecules).
- Micromolecules have molecular weights less than 1,000 daltons, while macromolecules have molecular weights above 10,000 daltons.
Chemical Composition of Living Tissues
- Water is the most abundant chemical in living organisms, making up 70-90% of the total cellular mass.
- Proteins make up 10-15% of the total cellular mass.
- Carbohydrates make up 3% of the total cellular mass.
- Lipids make up 2% of the total cellular mass.
- Nucleic acids make up 5-7% of the total cellular mass.
- Ions make up 1% of the total cellular mass.
Primary and Secondary Metabolites
- Primary metabolites are biomolecules that have identifiable functions and play known roles in normal physiological processes.
- Examples of primary metabolites include amino acids, sugars, and fatty acids.
- Secondary metabolites are biomolecules that do not have identifiable functions and roles in normal physiological processes.
- Examples of secondary metabolites include alkaloids, flavonoids, and antibiotics.
Biomacromolecules
- Biomacromolecules are large molecules that are found in the acid-insoluble fraction of living tissues.
- They include proteins, nucleic acids, polysaccharides, and lipids.
- Lipids are not strictly macromolecules, but are present in the acid-insoluble fraction due to their arrangement in structures like cell membranes.
Proteins
- Proteins are polypeptides, which are linear chains of amino acids linked by peptide bonds.
- There are 20 types of amino acids, making proteins heteropolymers.
- Proteins carry out many functions in living organisms, including:
- Transporting nutrients across cell membranes
- Fighting infectious organisms
- Acting as hormones
- Acting as enzymes
- Sensory reception
Polysaccharides
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Polysaccharides are long chains of sugars.
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They are found in the acid-insoluble fraction of living tissues.
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Examples of polysaccharides include:
- Cellulose (a homopolymer of glucose)
- Starch (a variant of cellulose found in plant tissues)
- Glycogen (a variant of starch found in animal tissues)
- Inulin (a polymer of fructose)
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Polysaccharides can have branches and can form helical secondary structures.
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Starch can hold I2 molecules in its helical portion, giving it a blue color.### Biomolecules
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Biomolecules are the building blocks of life, and they are classified into four main categories: carbohydrates, proteins, nucleic acids, and lipids.
Carbohydrates
- Cellulose is a complex polysaccharide found in plant cell walls.
- Chitin is a complex polysaccharide found in the exoskeletons of arthropods.
- Glycogen is a complex polysaccharide composed of glucose molecules, and its structure is illustrated in Figure 9.2.
Nucleic Acids
- Nucleic acids are polynucleotides composed of three chemically distinct components: a heterocyclic compound, a monosaccharide, and a phosphoric acid or phosphate.
- The heterocyclic compounds in nucleic acids are the nitrogenous bases: adenine, guanine, uracil, cytosine, and thymine.
- The sugar found in polynucleotides is either ribose (a monosaccharide pentose) or 2’ deoxyribose.
- Deoxyribonucleic acid (DNA) contains deoxyribose, while ribonucleic acid (RNA) contains ribose.
Proteins
- Proteins are heteropolymers containing strings of amino acids.
- The structure of proteins can be described at four levels: primary, secondary, tertiary, and quaternary.
- The primary structure of a protein refers to the sequence of amino acids.
- The secondary structure of a protein refers to the arrangement of amino acids in a helix or sheet.
- The tertiary structure of a protein refers to the three-dimensional arrangement of the polypeptide chain.
- The quaternary structure of a protein refers to the arrangement of multiple polypeptide chains (subunits) in a protein.
Enzymes
- Enzymes are proteins that catalyze specific chemical reactions.
- Enzymes have a primary structure, secondary structure, tertiary structure, and quaternary structure.
- The active site of an enzyme is a crevice or pocket that binds the substrate.
- Enzymes speed up chemical reactions by reducing the activation energy required.
- Enzymes are highly specific, and their activity is affected by temperature, pH, substrate concentration, and inhibitors.
Chemical Reactions
- Chemical reactions involve the breaking and forming of chemical bonds.
- The rate of a chemical reaction is the amount of product formed per unit time.
- Enzymes increase the rate of chemical reactions by catalyzing them.
Metabolic Pathways
- A metabolic pathway is a series of enzyme-catalyzed reactions that convert a substrate into a product.
- Metabolic pathways can lead to different end products depending on the conditions.
Enzyme Action
- The enzyme-substrate complex (ES) is formed when the substrate binds to the active site of the enzyme.
- The ES complex is short-lived and dissociates into the product and the unchanged enzyme.
- The catalytic cycle of an enzyme involves the binding of the substrate, the formation of the ES complex, and the release of the product.
Factors Affecting Enzyme Activity
- Enzyme activity is affected by temperature, pH, substrate concentration, and inhibitors.
- Each enzyme has an optimal temperature and pH at which it shows maximum activity.
- Enzyme activity is inhibited by competitive inhibitors, which bind to the active site and prevent the substrate from binding.
Classification and Nomenclature of Enzymes
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Enzymes are classified into six classes based on the type of reactions they catalyze.
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Each enzyme is given a unique four-digit number to identify it.### Enzymes Classification
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Transferases: catalyze the transfer of a group (G) between two substrates (S and S')
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Hydrolases: catalyze the hydrolysis of various bonds (ester, ether, peptide, glycosidic, C-C, C-halide, or P-N)
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Lyases: catalyze the removal of groups from substrates, leaving double bonds
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Isomerases: catalyze the inter-conversion of optical, geometric, or positional isomers
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Ligases: catalyze the linking of two compounds, forming bonds (C-O, C-S, C-N, P-O, etc.)
Co-factors
- Enzymes are composed of polypeptide chains, but may require non-protein constituents (co-factors) to be catalytically active
- Co-factors are bound to the apoenzyme (protein portion of the enzyme)
- Three types of co-factors: prosthetic groups, co-enzymes, and metal ions
Prosthetic Groups
- Organic compounds tightly bound to the apoenzyme
- Example: haem in peroxidase and catalase, which catalyze the breakdown of hydrogen peroxide
Co-enzymes
- Organic compounds with transient association with the apoenzyme
- Serve as co-factors in multiple enzyme-catalyzed reactions
- Often contain vitamins (e.g., NAD and NADP contain niacin)
Metal Ions
- Form coordination bonds with side chains at the active site and with the substrate
- Example: zinc is a co-factor for the proteolytic enzyme carboxypeptidase
Importance of Co-factors
- Catalytic activity is lost when the co-factor is removed from the enzyme
- Co-factors play a crucial role in the catalytic activity of the enzyme
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Description
Learn about the chemical composition and diversity of living organisms, including primary and secondary biomolecules.