Biology Chapter: Enzymes and Sugars

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Questions and Answers

What is the role of an enzyme in a chemical reaction?

  • To permanently change the substrate structure
  • To increase the activation energy required for the reaction
  • To act as a substrate in the reaction
  • To speed up the reaction by lowering activation energy (correct)

What happens to an enzyme when it is exposed to extreme pH levels?

  • It increases in size and mass
  • It becomes more effective at catalyzing reactions
  • It is destroyed or denatured (correct)
  • It changes the shape of the substrate

Which of the following best describes the lock and key model of enzyme action?

  • Enzyme can work with any substrate due to flexibility
  • Substrate fits exactly into a specific active site (correct)
  • Enzyme changes shape to fit the substrate
  • Active site can accommodate multiple substrates at once

What distinguishes aldose sugars from ketose sugars?

<p>Aldose sugars have their carbonyl group located at the end of the carbon chain. (C)</p> Signup and view all the answers

What is the optimum pH level for pepsin, an enzyme found in the stomach?

<p>pH 3 (D)</p> Signup and view all the answers

Which sugar is an example of a triose?

<p>Glyceraldehyde (C)</p> Signup and view all the answers

How does the specificity of an enzyme relate to its active site?

<p>The active site matches the shape of only a specific substrate (C)</p> Signup and view all the answers

How many carbon atoms are in pentose sugars?

<p>5 C atoms (B)</p> Signup and view all the answers

What is a common feature of glucose, galactose, and fructose?

<p>They share the same molecular formula but differ in structure. (A)</p> Signup and view all the answers

Which functional group is characteristic of monosaccharides?

<p>Carbonyl group (C=O) (C)</p> Signup and view all the answers

Which of the following fatty acids can be synthesized by the body?

<p>Linolenic acid (A), Linoleic acid (B), Arachidonic acid (D)</p> Signup and view all the answers

What is the primary function of triglycerides in the body?

<p>Energy storage (A), Providing insulation (C)</p> Signup and view all the answers

What basic structure composes a phospholipid?

<p>1 glycerol, 2 fatty acids, and 1 phosphate group (D)</p> Signup and view all the answers

Which of the following statements is true regarding non-essential amino acids?

<p>They can be synthesized by the body. (C)</p> Signup and view all the answers

What is the main component responsible for providing buoyancy in aquatic animals?

<p>Triglycerides (A)</p> Signup and view all the answers

Which process describes the formation of a dipeptide?

<p>Removal of water from two amino acids (C), Joining two amino acids with a peptide bond (D)</p> Signup and view all the answers

What differentiates essential amino acids from non-essential amino acids?

<p>Essential amino acids need to be obtained from food. (C)</p> Signup and view all the answers

Which molecule is indicated as the major component of cell membranes?

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

What characterizes quaternary protein structure?

<p>It is formed by the joining of two or more polypeptide chains. (B)</p> Signup and view all the answers

Which of the following is NOT a bond that occurs in tertiary or quaternary protein structures?

<p>Peptide bond (D)</p> Signup and view all the answers

Which type of protein predominantly forms long, parallel filaments or strands?

<p>Fibrous proteins (A)</p> Signup and view all the answers

What role do fibrous proteins primarily serve in biological systems?

<p>Mechanical and structural support (A)</p> Signup and view all the answers

Which of the following does NOT describe globular proteins?

<p>They consist primarily of a secondary structure. (D)</p> Signup and view all the answers

Which specific protein is an example of quaternary structure?

<p>Hemoglobin (C)</p> Signup and view all the answers

What type of interaction occurs primarily between R groups in proteins?

<p>Hydrophobic (van der Waals) interaction (A)</p> Signup and view all the answers

How are proteins classified based on their structure?

<p>Fibrous, globular, and conjugated (D)</p> Signup and view all the answers

What is the primary role of an enzyme in biochemical reactions?

<p>To act as a biological catalyst (B)</p> Signup and view all the answers

Which statement best describes the specificity of enzymes?

<p>Each enzyme is specific to a particular substrate (A)</p> Signup and view all the answers

In the induced fit model, what happens when the substrate binds to the enzyme?

<p>The active site undergoes a conformational change to fit the substrate (D)</p> Signup and view all the answers

Which factor is NOT typically a direct influence on enzyme activity?

<p>Color of the enzyme (D)</p> Signup and view all the answers

What distinguishes a reversible catalyst from an irreversible catalyst?

<p>Reversible catalysts can bind and release substrates multiple times (D)</p> Signup and view all the answers

What is the primary difference between DNA and RNA regarding their structure?

<p>DNA consists of two polynucleotide chains twisted into a double helix. (A)</p> Signup and view all the answers

Which base pairing rules apply in DNA?

<p>Adenine pairs with thymine and cytosine pairs with guanine. (C)</p> Signup and view all the answers

What connects two nucleotides in a dinucleotide?

<p>Phosphodiester bonds between the OH groups. (D)</p> Signup and view all the answers

What is the role of DNA in living organisms?

<p>DNA carries genetic information that controls the activities of a cell. (D)</p> Signup and view all the answers

How are adenine and thymine held together in DNA?

<p>By two hydrogen bonds. (C)</p> Signup and view all the answers

What process is used to break down nucleotides in DNA?

<p>Hydrolysis. (C)</p> Signup and view all the answers

Which components make up the backbone of a DNA strand?

<p>Sugar and phosphate units. (D)</p> Signup and view all the answers

What type of bonds hold the complementary base pairs of DNA together?

<p>Hydrogen bonds. (B)</p> Signup and view all the answers

Flashcards

Enzyme

A biological catalyst produced by living cells that speeds up the rate of a chemical reaction by lowering the activation energy.

Activation Energy

The minimum amount of energy required by a reactant (substrate) to start a chemical reaction.

Active Site

A specific site on an enzyme where the substrate binds.

Enzyme Denaturation

A change in the shape of an enzyme, often caused by extreme temperatures or pH, that makes it lose its ability to function.

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Lock and Key Model

A model of enzyme action where the substrate fits perfectly into the active site of the enzyme.

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Substrate

The molecule upon which an enzyme acts.

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Induced Fit Model

The model that describes how an enzyme's active site changes shape to fit the substrate.

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Factors Affecting Enzyme Reactions

Factors that influence the rate of enzyme-catalyzed reactions, such as temperature, pH, and substrate concentration.

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Lipids

A group of hydrophobic molecules that are insoluble in water. They are primarily composed of carbon and hydrogen atoms with a small amount of oxygen.

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Fats/Triglycerides/Triacylglycerol

A type of lipid that is the most abundant in the body. It's composed of one glycerol molecule and three fatty acid chains.

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Glycerol/Glycerine

A 3-carbon alcohol with three hydroxyl groups. It's soluble in water.

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Fatty Acids

Long chains of carbon atoms with a carboxyl group at one end. They can be saturated (no double bonds) or unsaturated (have double bonds).

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Phospholipids

A type of lipid that is a major component of cell membranes. It's an amphipathic molecule, meaning it has both hydrophilic (water-loving) and hydrophobic (water-fearing) parts.

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Steroids

A type of lipid that includes cholesterol, hormones, and vitamins. They have a characteristic four-ring structure.

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Proteins

A group of compounds composed of amino acids linked together by peptide bonds. They play a vital role in various biological functions, including building and repairing tissues, transporting substances, and catalyzing reactions.

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Essential Amino Acids

Amino acids that cannot be synthesized by the body and must be obtained through diet or supplements.

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Aldose sugars

Sugar molecules with a carbonyl group located at the end of the carbon chain. Examples include glucose.

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Ketose sugars

Sugar molecules with a carbonyl group located in the middle of the carbon chain. Examples include fructose.

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Triose sugars

Sugars containing 3 carbon atoms. Examples include glyceraldehyde and dihydroxyacetone.

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Pentose sugars

Sugars containing 5 carbon atoms. Examples include ribose, ribulose, and deoxyribose.

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Hexose sugars

Sugars containing 6 carbon atoms. Examples include glucose and fructose.

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Adenine (A)

A nitrogenous base found in both DNA and RNA, pairing with thymine (T) in DNA and uracil (U) in RNA.

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Dinucleotide

A molecule consisting of two nucleotides joined together by a phosphodiester bond.

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Formation of polypeptide

The process of joining multiple nucleotides together to create a long chain (polynucleotide).

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DNA Structure

A structural component of DNA, characterized by a double helix formed by two polynucleotide chains held together by hydrogen bonds.

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Nitrogenous bases in DNA

Guanine, Adenine, Thymine, Cytosine are the four nitrogenous bases found in DNA.

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RNA

RNA is a single-stranded molecule that carries genetic information from DNA to ribosomes for protein synthesis.

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Hydrolysis

A process that breaks down a polypeptide into individual nucleotides.

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Base pairing rule

The specific pairing of nitrogenous bases in DNA — adenine pairs with thymine (A-T), and guanine pairs with cytosine (G-C).

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Peptide Bond

The type of bond that holds amino acid residues together in a polypeptide chain. It forms by a reaction between the carboxyl group of one amino acid and the amino group of another.

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Hierarchy of Protein Structure

The four levels of protein structure: primary, secondary, tertiary, and quaternary. These levels describe the organization and folding of a protein from its linear sequence of amino acids to its complex 3D shape.

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Primary Protein Structure

The first level of protein structure, describing the linear sequence of amino acids in a polypeptide chain.

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Secondary Protein Structure

The second level of protein structure, characterized by local regular patterns formed by hydrogen bonding. Common forms include alpha helices and beta sheets.

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Tertiary Protein Structure

The third level of protein structure, describing the overall three-dimensional shape of a protein. This is influenced by interactions between amino acid side chains.

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Quaternary Protein Structure

The fourth level of protein structure, formed when multiple polypeptide chains assemble together to create a functional protein complex.

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Fibrous Proteins

Proteins that are generally elongated, insoluble in water, and play structural or mechanical roles in cells and tissues.

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Globular Proteins

Proteins that are generally spherical, soluble in water, and often involved in catalysis, transport, and other dynamic processes.

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Study Notes

Biological Molecules

  • Biological macromolecules are the building blocks of all living things
  • Polymers are molecules made up of multiple monomers
  • Four major types of biological macromolecules include carbohydrates, lipids, proteins, and nucleic acids

Carbohydrates

  • Composed of carbon, hydrogen, and oxygen atoms
  • Ratio of C:H:O is approximately 1:2:1 (CHâ‚‚O)n
  • Monosaccharides are simple sugars with 3-7 carbon atoms
  • Disaccharides are formed by two monosaccharides joined by a glycosidic bond
  • Polysaccharides are polymers of monosaccharides
  • Functions include energy storage and structural support

Lipids

  • Consist mainly of carbon and hydrogen atoms with few oxygen atoms
  • Hydrophobic molecules, insoluble in water
  • Major types: fats, phospholipids, and steroids
  • Fats are triglycerides, formed from glycerol and three fatty acids
  • Phospholipids are amphipathic, containing hydrophilic heads and hydrophobic tails
  • Steroids have a distinct four-ring structure

Proteins

  • Polymers formed from amino acid monomers
  • Amino acids have a central carbon atom bonded to hydrogen, an amino group, a carboxyl group, and a variable R group
  • Twenty types of amino acids combine in varying sequences to make the unique proteins within organisms
  • Dipeptides and polypeptides are formed from multiple amino acids joined by peptide bonds
  • Proteins can have a primary, secondary, tertiary, or quaternary structure, which determines their function
  • Function in a wide range of functions within organisms including transport, structural support, and catalysis

Nucleic Acids

  • Polymers of nucleotides
  • Nucleotides consist of a pentose sugar (either ribose or deoxyribose), a nitrogenous base (adenine, thymine, guanine, cytosine, or uracil), and a phosphate group
  • DNA has two polynucleotide chains arranged antiparallel that form a double helix structure
  • RNA is a single stranded polynucleotide made up of ribose, uracil, guanine, adenine, and cytosine

ATP

  • Adenosine triphosphate
  • Composed of adenine, ribose, and three phosphate groups
  • High energy phosphate bonds
  • Releases energy when a phosphate bond is broken to form ADP (adenosine diphosphate)
  • Functions as an energy carrier for biological processes

Water

  • Polar molecule with unequal sharing of electrons, thus creating a slightly positive charge on one side and a slightly negatively charged side
  • Holds together via hydrogen bonds
  • Important properties include high specific heat capacity, high latent heat of vaporisation and high surface tension and maximum density at 4°C

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