Biology Chapter Enzymes and Carbohydrates
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Questions and Answers

What component is essential for enzyme activity that is not a protein?

  • Substrate
  • Inhibitor
  • Cofactor (correct)
  • Regulator

Which of the following is a common feature of most enzymes?

  • They are proteins (correct)
  • They contain nucleic acids
  • They are carbohydrates
  • They are lipids

What suffix is commonly found in the names of enzymes?

  • -in
  • - peptide
  • -ase (correct)
  • -ose

Which enzyme class is specifically involved in hydrolysis reactions?

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

What structural characteristic is primarily responsible for enzyme specificity?

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

Which amino acid is known for containing sulfur and is important in protein structure?

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

What is the term for the model that describes the fit between an enzyme's active site and its substrate?

<p>Induced fit model (C)</p> Signup and view all the answers

Which of the following roles does a cofactor NOT have in enzyme activity?

<p>Acting as a competitive inhibitor (A)</p> Signup and view all the answers

Which polysaccharide cannot be digested by humans?

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

Which sugar alcohol is primarily utilized as a sweetener in chewing gum?

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

Which polysaccharide serves a structural function in cartilage?

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

Which enzyme is responsible for breaking down sucrose into glucose and fructose?

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

What is the primary function of glycoproteins in biological systems?

<p>Cell-cell recognition and communication (A)</p> Signup and view all the answers

What type of carbohydrate constitutes dietary fiber?

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

What can be a consequence of insufficient dietary fiber intake?

<p>Increased plaque formation (C)</p> Signup and view all the answers

Which glycosaminoglycan functions as an anticoagulant?

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

What type of mutation involves substituting one nucleotide for another?

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

Which component forms the backbone of DNA?

<p>Sugar-phosphate groups (A)</p> Signup and view all the answers

What is the term for the sequence written from the 5′ to 3′ end?

<p>Nucleic acid sequence (A)</p> Signup and view all the answers

Which class of enzymes is responsible for catalyzing the rearrangement of atoms within a molecule?

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

In the context of mRNA, what does the 'A' stand for?

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

Which type of DNA repair mechanism removes up to 24-32 nucleotides?

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

What is the primary function of transferases in enzymatic processes?

<p>Facilitate the transfer of functional groups (B)</p> Signup and view all the answers

What is the three-dimensional structure of tRNA characterized as?

<p>L-shaped (C)</p> Signup and view all the answers

Which enzyme is characterized by its specific action on L-amino acids?

<p>L-amino acid oxidase (B)</p> Signup and view all the answers

What type of reaction do ligases primarily catalyze?

<p>Bond formation using ATP (B)</p> Signup and view all the answers

What is the primary role of mRNA during protein synthesis?

<p>To carry the genetic template (A)</p> Signup and view all the answers

Which repair mechanism is primarily tasked with correcting bulky DNA lesions?

<p>Nucleotide excision repair (NER) (D)</p> Signup and view all the answers

Phosphatases are enzymes that exhibit which type of specificity?

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

Which enzyme would primarily be responsible for removing a carboxyl group from a substrate?

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

What creates the major and minor grooves in the DNA double helix?

<p>The twisting of the helix (D)</p> Signup and view all the answers

Which specificity describes enzymes that act only on a single substrate?

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

What is the function of the sugar-phosphate backbone?

<p>It provides structural support. (A)</p> Signup and view all the answers

In enzymatic reactions, what describes the specificity for substrate types rather than specific molecules?

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

How many base pairs are found in one complete turn of a DNA helix?

<p>10 (A)</p> Signup and view all the answers

Which enzyme unwinds the DNA double helix during replication?

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

What are Okazaki fragments?

<p>Short DNA fragments synthesized on the lagging strand (A)</p> Signup and view all the answers

What is the function of DNA polymerase?

<p>To add nucleotides to the growing DNA strand (C)</p> Signup and view all the answers

DNA replication is characterized as which of the following?

<p>Semi-conservative (C)</p> Signup and view all the answers

Which enzyme seals nicks in the sugar-phosphate backbone?

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

What happens to enzyme activity when substrate concentration is increased at a constant enzyme concentration?

<p>It will eventually saturate the enzyme (C)</p> Signup and view all the answers

What is the optimum temperature for most human enzymes?

<p>37°C (B)</p> Signup and view all the answers

What is the optimal pH level for pepsin to function effectively in the stomach?

<p>2.0 (C)</p> Signup and view all the answers

According to the lock-and-key model, what is true about the active site of an enzyme?

<p>The active site has a fixed shape (A)</p> Signup and view all the answers

Which model explains the flexibility of the enzyme's active site?

<p>Induced fit model (A)</p> Signup and view all the answers

What characteristic defines a competitive inhibitor in enzymatic reactions?

<p>It resembles the substrate (B)</p> Signup and view all the answers

Which statement accurately describes noncompetitive inhibitors?

<p>They change the enzyme's shape (A)</p> Signup and view all the answers

What effect does increasing substrate concentration have at low Michaelis-Menten kinetics?

<p>Increases enzyme activity linearly (A)</p> Signup and view all the answers

Flashcards

What polysaccharide can't humans digest?

Cellulose is a polysaccharide that humans cannot digest due to the lack of the necessary enzyme to break down its beta-1,4 glycosidic bonds.

Which sugar alcohol is in chewing gum?

Sorbitol is a sugar alcohol commonly used as a sweetener in chewing gum because of its low glycemic index and pleasant taste.

What's in cartilage?

Chondroitin sulfate is a glycosaminoglycan that plays a structural role in cartilage, contributing to its flexibility and resilience.

Which enzyme breaks down sucrose?

Sucrase is an enzyme that breaks down sucrose (table sugar) into glucose and fructose. It's found in the small intestine.

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What do glycoproteins do?

Glycoproteins are proteins that have carbohydrate chains attached to them. Their key role is in cell-cell recognition and communication, allowing cells to interact and communicate.

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What is dietary fiber?

Dietary fiber is made up of indigestible carbohydrates. It comes from plant sources and is important for digestive health.

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What happens if you lack fiber?

Lack of dietary fiber can lead to increased plaque formation in the arteries, contributing to heart disease.

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What is heparin?

Heparin is a glycosaminoglycan with anticoagulant properties. It prevents blood clotting by inhibiting the activity of certain clotting factors.

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Amino Acid Sequence

The unique sequence of amino acids in a protein chain. It's like the 'recipe' for building the protein.

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Protein Structure

The three-dimensional shape of a protein, formed by folding and twisting of the amino acid chain. It's crucial for the protein's function.

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Number of Peptide Bonds

The number of connections (peptide bonds) between individual amino acid units in a protein. It gives us a sense of the protein's size.

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Polarity

The property of a molecule based on its charge distribution. It affects how a protein interacts with water and other molecules.

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Sulfur-Containing Amino Acid

An amino acid that contains sulfur in its structure.

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Enzymes

Biological catalysts - molecules that accelerate chemical reactions in living organisms without being consumed.

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Cofactors

Non-protein molecules that assist enzymes in their activity. They are like helpers or tools.

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Enzyme Suffix: -ase

A common suffix in enzyme names, signifying they're catalysts.

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Transferases

Enzymes that catalyze the transfer of a functional group from one molecule to another.

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Isomerases

Enzymes that catalyze the rearrangement of atoms within a molecule, changing its structure.

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Decarboxylases

Enzymes that catalyze the removal of a carboxyl group (COOH) from a molecule.

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Ligases

Enzymes that catalyze bond formation, often using ATP as an energy source.

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Absolute Specificity

The highest level of enzyme specificity, where an enzyme acts on only one specific substrate.

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Group Specificity

Enzymes that act on molecules with specific functional groups, like phosphates.

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Linkage Specificity

Enzymes that recognize and act on specific chemical bonds within a molecule.

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Stereochemical Specificity

A type of enzyme specificity where the enzyme can distinguish between enantiomers (mirror images) of a molecule.

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Enzyme Saturation

Increasing substrate concentration will eventually reach a point where all enzyme active sites are occupied, leading to no further increase in reaction rate.

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Optimum Temperature

The temperature at which an enzyme exhibits maximum activity.

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Optimum pH

The pH at which an enzyme functions most effectively.

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Lock-and-Key Model

A model suggesting the active site of an enzyme has a rigid shape that perfectly matches the substrate.

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Induced Fit Model

The active site of an enzyme is flexible and undergoes a change in shape to accommodate the substrate.

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Competitive Inhibitor

A type of enzyme inhibitor that resembles the substrate and binds to the active site, competing with the substrate for binding.

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Noncompetitive Inhibitor

A type of enzyme inhibitor that binds to a site other than the active site, altering the enzyme's shape and reducing its activity.

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Factors Affecting Enzyme Activity

Factors that can influence enzyme activity, such as temperature, pH, substrate concentration, and enzyme concentration.

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What creates the major and minor grooves in DNA?

The twisting of the DNA double helix creates major and minor grooves.

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What is the function of the sugar-phosphate backbone in DNA?

The sugar-phosphate backbone provides structural support for the DNA molecule, holding the nitrogenous bases together.

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How many base pairs are in one turn of a DNA helix?

There are 10 base pairs in one complete turn of a DNA helix.

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Which enzyme unwinds DNA during replication?

Helicase is the enzyme responsible for unwinding the DNA double helix during replication.

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What are Okazaki fragments?

Okazaki fragments are short DNA segments synthesized on the lagging strand during replication.

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What is the function of DNA polymerase?

DNA polymerase is the enzyme that adds nucleotides to the growing DNA strand during replication.

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What type of process is DNA replication?

DNA replication is semi-conservative, meaning each new DNA molecule contains one original strand and one newly synthesized strand.

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Which enzyme seals nicks in DNA?

Ligase is the enzyme that seals nicks in the sugar-phosphate backbone of DNA during replication.

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What's a point mutation?

A point mutation is a type of genetic alteration that involves the substitution of a single nucleotide for another within a DNA sequence.

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What forms the DNA backbone?

The sugar-phosphate backbone serves as the structural foundation of DNA and RNA molecules, providing a framework for the arrangement of nucleotides.

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What's a nucleic acid sequence?

The sequence written from the 5′ to 3′ end of a DNA or RNA molecule is known as the nucleic acid sequence.

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What does mRNA stand for?

mRNA stands for messenger RNA, its role is to carry genetic information from DNA in the nucleus to the ribosomes in the cytoplasm, where it directs the synthesis of proteins.

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How does NER repair DNA?

Nucleotide excision repair (NER) is a DNA repair mechanism that removes and replaces a segment of DNA containing up to 24-32 nucleotides, often involving bulky or damaged DNA sections.

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What is the 3D shape of tRNA?

tRNA (transfer RNA) adopts a three-dimensional L-shaped structure which is crucial for its role in protein synthesis. It recognizes specific codons in mRNA and delivers the corresponding amino acids to the ribosome.

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What is a frameshift mutation?

A frameshift mutation is a genetic alteration that involves the insertion or deletion of nucleotides within a DNA sequence, shifting the reading frame of the genetic code.

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What's a codon?

A codon is a three-nucleotide sequence in mRNA that specifies a particular amino acid during protein synthesis.

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Study Notes

Biochemistry - Finals Practice Questions

  • Biochemistry: The study of the structure and function of biomolecules
  • Bioorganic substances: Carbohydrates, lipids, proteins, nucleic acids
  • Lipids' function: Forming cell membranes, serving as an energy source, acting as chemical messengers; NOT catalyzing reactions
  • Enzymes' function: Catalyzing and accelerating chemical reactions
  • Cell's powerhouse: Mitochondria
  • Protein synthesis location: Ribosomes
  • Nucleic acids' role: Storing genetic information and directing protein synthesis
  • Cell membrane's purpose: Separating the internal environment from the external environment
  • Metabolism: The set of life-sustaining chemical reactions in organisms
  • Organelle for packaging and distribution of proteins: Golgi apparatus
  • Molecule responsible for catalyzing reactions in cells: Proteins
  • Photosynthesis location: Chloroplasts
  • Lysosomes' function: Digesting unwanted materials in the cell
  • Endoplasmic reticulum's function: Protein and lipid synthesis
  • Nucleus' contents: Genetic material (DNA)
  • Cell membrane structure: Bilayer of phospholipids
  • Peroxisomes' function: Breakdown of hydrogen peroxide
  • Common elements in living organisms: Carbon, oxygen, nitrogen
  • Oxidation-reduction reaction in metabolism: Transfer of electrons between molecules
  • Information center of the cell: Nucleus
  • Most abundant molecule in living cells: Water
  • Bond connecting nucleotides in DNA: Phosphodiester bonds
  • Carbohydrates' primary role: Providing energy
  • Main structural component of cell membranes: Lipids
  • Primary glucose storage in animals: Glycogen
  • Enzyme property (NOT): Being consumed during a reaction; enzymes are reusable
  • Type of molecule ATP is: Nucleotide
  • Process that breaks down glucose for energy: Glycolysis
  • Location of oxidative phosphorylation: Mitochondria
  • Amino acid description: Building block of proteins
  • RNA's role in protein synthesis: Transporting amino acids to ribosomes
  • Plant cell structure (NOT in animal cells): Cell wall
  • Part of the enzyme that binds to the substrate: Active site
  • Function of chloroplasts: Photosynthesis
  • Molecule carrying genetic code from nucleus to ribosome: mRNA
  • Backbone of a protein molecule composed of: Amino acids
  • Molecule primarily involved in long-term energy storage: Fatty acids
  • Function of the Golgi apparatus: Modifying and packaging proteins
  • NOT a function of nucleic acids: Providing cellular energy
  • Cholesterol's role in cell membranes: Maintaining membrane fluidity
  • "Bad cholesterol": LDL (low-density lipoprotein)
  • Eicosanoids derived from: Arachidonic acid
  • Essential fatty acid: Linoleic acid
  • Beneficial fat for diet: Monounsaturated fats
  • Artificial fat substitute: Olestra
  • Lipid-soluble vitamin involved in blood clotting: Vitamin K
  • Lipid transporting cholesterol from the liver: LDL
  • Lipid class of wax: Biological waxes
  • Process converting oils to solid fats: Hydrogenation
  • Enzyme digesting starch in humans: Amylase
  • Polysaccharide in arthropod exoskeletons: Chitin
  • Sugar alcohol sweetener: Sorbitol
  • Polysaccharide in cartilage: Chondroitin sulfate
  • Enzyme breaking down sucrose: Sucrase
  • General role of glycoproteins: Cell-cell recognition and communication
  • Dietary fiber source: Indigestible carbohydrates
  • Consequence of lack of dietary fiber: Increased digestive plaque formation
  • Glycosaminoglycan as anticoagulant: Heparin
  • Definition of a lipid: An organic compound insoluble in water but soluble in non-polar solvents

Carbohydrates Study Notes

  • Carbohydrate classification: Polyhydroxyaldehydes or polyhydroxyketones
  • Carbohydrate function (NOT): Storing genetic information
  • Empirical formula of carbohydrates: CnH2nOn
  • Simplest form of carbohydrates: Monosaccharides
  • Glucose classification: Aldohexose
  • Disaccharide in milk: Lactose
  • Cellulose linkage: β-1,4-glycosidic
  • Sweetest sugar: Fructose
  • Glycogen function: Long-term energy storage in animals
  • Primary structural polysaccharide in plants: Cellulose
  • RNA component sugar: Ribose
  • Blood sugar molecule: Glucose
  • Bond forming between monosaccharides: Glycosidic bond (specifically, condensation or dehydration reaction)
  • Reducing disaccharide in beer/germinating grains: Maltose
  • Non-reducing sugar: Sucrose
  • Polysaccharide turning blue with iodine: Starch
  • Glucose storage in animals: Glycogen
  • Glycosidic bond in sucrose: α-1,2-glycosidic
  • Homopolysaccharide examples: Starch, glycogen, cellulose (and others)
  • Cellulose repeating unit: D-glucose
  • Amylopectin characteristic (NOT): Having β-1,4-glycosidic bonds
  • Enzyme digesting starch in humans: Amylase
  • Sugar derivative from reducing glucose: Sorbitol (Glucitol)
  • Joint lubricant polysaccharide: Hyaluronic acid

Lipids Study Notes

  • Lipid Definition: An organic compound insoluble in water but soluble in non-polar solvents
  • Lipid classifications (NOT): Vitamins
  • Triacylglycerol function: Energy storage
  • Membrane lipids: Phospholipids
  • Steroid hormone: Cholesterol
  • Saturated fatty acid: Stearic acid
  • Polyunsaturated fatty acid: Having two or more double bonds
  • Omega-3 fatty acids: Role in heart health and inflammation reduction
  • Main component of biological membranes: Phospholipids
  • Key structural feature of phospholipid: Two fatty acids and a phosphate group attached to glycerol
  • Steroid: Cholesterol
  • Bile acids' role in lipid digestion: Emulsification of dietary fats
  • Essential fatty acid: Linoleic acid
  • Cholesterol role in cell membranes: Maintaining membrane fluidity
  • "Bad cholesterol": LDL (low-density lipoprotein)
  • Eicosanoids source: Arachidonic acid
  • Eicosanoids' function(NOT): Producing ATP
  • Steroid hormones' function: Regulating reproduction and secondary sex characteristics
  • Component of biological waxes: Fatty acids and long-chain alcohols
  • "Antioxidant vitamin": Vitamin E
  • Cause of lipid rancidity: Oxidation of unsaturated fatty acids
  • Lipid class involved in cellular signaling and immune responses: Eicosanoids
  • Essential lipid for vitamin D production: Cholesterol
  • Lipid involved in emulsification of fats during digestion: Bile acids
  • Lipid disorder characterized by high LDL: Hypercholesterolemia
  • Lipid important for myelin sheath: Sphingomyelin
  • Lipid promoting inflammation and allergic responses: Leukotriene
  • Product of triacylglycerol saponification: Glycerol and fatty acid salts
  • "Good cholesterol": HDL (high-density lipoprotein)
  • Triglyceride backbone: Glycerol

Proteins Study Notes

  • Protein composition: Amino acids
  • Protein mass percentage after water: 15%
  • Protein element NOT commonly found: Silicon
  • Protein containing only amino acids: Simple protein
  • Protein class including albumin: Simple protein
  • Fibrous protein example: Collagen
  • Myoglobin function: Storing oxygen in muscles
  • Insulin type of protein: Messenger protein
  • Essential amino acid: Lysine
  • Protein for oxygen transport: Hemoglobin
  • Protein storing iron: Ferritin
  • Protein for movement: Myosin
  • Bond linking amino acids in protein: Peptide bond
  • Secondary protein structure (NOT): Tertiary coil
  • Bond holding alpha-helix structure: Hydrogen bonds
  • Protein with prosthetic group: Conjugated protein
  • Achiral amino acid: Glycine
  • Protein structure determining function: Tertiary structure
  • Bond stabilizing secondary structures: Hydrogen bonds
  • Amino acid with sulfur: Cysteine
  • Type of molecule an enzyme is: Protein
  • Protein for hard body covering: Keratin
  • Storage form of glucose in animals: Glycogen

Enzymes Study Notes

  • Enzyme composition: Primarily proteins
  • Cofactor role: Necessary for enzyme activity
  • Enzyme suffix: -ase
  • Hydrolysis-catalyzing enzyme class: Hydrolases
  • Enzyme active site model: Induced Fit Model
  • Enzyme regulation (NOT): Passive regulation
  • Enzyme active site: Region where substrate binds and catalysis occurs, specifically, the active site of the enzyme
  • Effect of high temperature on enzymes (NOT): becoming more active
  • Enzyme regulation mechanism: Feedback inhibition
  • Enzyme inhibitor that resembles substrate: Competitive inhibitor
  • Enzyme inhibitor changing enzyme shape: Noncompetitive inhibitor
  • Effect of increasing enzyme concentration: Increased enzyme activity
  • Maximal enzyme activity point due to substrate saturation: Enzyme saturation

Nucleic Acids Study Notes

  • DNA/RNA repeating unit: Nucleotide
  • RNA sugar: Ribose
  • DNA sugar: Deoxyribose
  • Base pairing with guanine (G) in DNA: Cytosine (C)
  • DNA double helix diameter: ~2 nm
  • RNA that carries amino acids to the ribosome: tRNA
  • Enzyme during transcription: RNA polymerase
  • Process copying DNA into an identical strand: Replication
  • Mutation replacing one nucleotide for another: Point mutation
  • DNA backbone: Sugar-phosphate groups
  • DNA end sequence from 5' to 3': Nucleic acid sequence
  • Messenger RNA abbreviation: mRNA
  • Base unique to RNA: Uracil
  • Enzyme sealing nicks in DNA: DNA ligase
  • T/RNA shape in 3D: L-shaped
  • Codon length: Three nucleotides
  • Genetic code degeneracy meaning: Multiple codons code for the same amino acid
  • Termination sequence in protein synthesis: Stop codons (e.g., UAA, UAG, UGA)
  • Enzyme that unwinds DNA: Helicase

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Test your knowledge on enzymes and carbohydrates with this quiz. Explore essential components for enzyme activity, structural characteristics, and classifications within biological systems. Perfect for students studying biology at various levels.

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