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Quizzes > Science > Biology

Master Biomolecules: Enzymes, Carbohydrates, Lipids & Proteins Quiz

Ready for a challenge? Prove you know which category enzymes belong in and more with our biomolecules test!

Difficulty: Moderate
2-5mins
Learning OutcomesCheat Sheet
Paper art biomolecule icons for quiz on enzymes, carbohydrates, lipids, proteins on sky blue background

Ready to tackle the ultimate biomolecules test? Whether you're prepping for a biochemistry enzymes test or eager to master macromolecules, this engaging free quiz on enzymes, carbohydrates, lipids, and proteins has you covered. In this biomolecules quiz, you'll answer key questions - from identifying enzymes which can speed up reactions belong in what category to acing an enzymes quiz or full biomolecules exam. Perfect for students, DIY learners, and curious minds, you'll strengthen your grasp of molecular structures and reaction rates. Spark your scientific curiosity and measure your mastery - take the challenge now! Explore biomolecules and enzymes

Which of the following is the monomer unit of proteins?
Monosaccharides
Fatty acids
Amino acids
Nucleotides
Proteins are polymers formed by amino acids linked via peptide bonds in a process called dehydration synthesis. Each amino acid contains an amino group, carboxyl group, and unique side chain which determines its properties. The order and composition of these amino acids affect the protein's structure and function in cells. https://en.wikipedia.org/wiki/Amino_acid
What is the primary role of enzymes in biochemical reactions?
Energy storage molecules
Structural support in cell membranes
Genetic information carriers
Biological catalysts
Enzymes are biological catalysts that accelerate chemical reactions by lowering the activation energy required for the reaction. They bind substrates to their active site, often forming transient enzyme - substrate complexes. Despite facilitating the reaction, enzymes remain unchanged and can be reused multiple times. https://en.wikipedia.org/wiki/Enzyme
Which of the following sugars is a monosaccharide?
Sucrose
Cellulose
Lactose
Glucose
Glucose is a simple sugar classified as a monosaccharide because it cannot be hydrolyzed into simpler sugars. It serves as a primary energy source for cells and is involved in cellular respiration. Other sugars like sucrose and lactose are disaccharides composed of two monosaccharides linked together. https://en.wikipedia.org/wiki/Glucose
What type of bond links amino acids together in proteins?
Glycosidic bond
Ester bond
Phosphodiester bond
Peptide bond
Peptide bonds form via a dehydration synthesis reaction, linking the carboxyl group of one amino acid to the amino group of the next. These covalent bonds create the backbone of protein structures. Breaking peptide bonds requires proteolytic enzymes through hydrolysis. https://en.wikipedia.org/wiki/Peptide_bond
Starch belongs to which class of biomolecules?
Lipid
Protein
Carbohydrate
Nucleic acid
Starch is a polysaccharide made from glucose units connected by ?-1,4 and ?-1,6 glycosidic bonds. It serves as the main energy storage molecule in plants. Humans can digest starch using amylase enzymes located in saliva and the pancreas. https://en.wikipedia.org/wiki/Starch
Which of the following best describes competitive enzyme inhibition?
Binds to the active site and competes with substrate
Binds to an allosteric site and decreases Vmax
Irreversibly inactivates the enzyme
Lowers Km without affecting Vmax
Competitive inhibitors resemble the substrate and bind to the enzyme's active site, blocking substrate binding. This increases the apparent Km (reduces enzyme - substrate affinity) but does not change the maximum velocity (Vmax) if sufficient substrate is present. Competitive inhibition can be overcome by increasing substrate concentration. https://en.wikipedia.org/wiki/Enzyme_inhibitor#Competitive_inhibition
Which level of protein structure is characterized by ?-helices and ?-pleated sheets?
Primary structure
Quaternary structure
Secondary structure
Tertiary structure
The secondary structure of proteins is formed by hydrogen bonds between backbone amide hydrogen and carbonyl oxygen atoms. Common secondary structures include ?-helices and ?-pleated sheets. These local conformations contribute to overall protein folding and stability. https://en.wikipedia.org/wiki/Protein_secondary_structure
Which class of lipid is amphipathic and forms the bilayer of cell membranes?
Waxes
Steroids
Phospholipids
Triglycerides
Phospholipids consist of hydrophilic head groups and two hydrophobic fatty acid tails, making them amphipathic. In aqueous environments, they assemble into bilayers that form the basic structure of cell membranes. This arrangement creates a selective barrier for ions and molecules. https://en.wikipedia.org/wiki/Phospholipid
Which enzyme catalyzes the phosphorylation of fructose-6-phosphate in glycolysis?
Pyruvate kinase
Aldolase
Hexokinase
Phosphofructokinase-1
Phosphofructokinase-1 (PFK-1) catalyzes the irreversible phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate in glycolysis. It is a key regulatory step and is allosterically regulated by ATP, AMP, and citrate. Regulation of PFK-1 helps balance energy production in the cell. https://en.wikipedia.org/wiki/Phosphofructokinase
Which model describes enzyme binding after a conformational change upon substrate interaction?
Lock-and-key model
Transition state model
Induced fit model
Allosteric model
The induced fit model proposes that enzyme active sites are flexible and reshape to fit the substrate upon binding. This conformational change enhances the enzyme's ability to catalyze the reaction. The model contrasts with the rigid lock-and-key hypothesis. https://en.wikipedia.org/wiki/Induced_fit
What type of glycosidic linkage connects glucose units in cellulose?
?-1,4-glycosidic bond
?-1,6-glycosidic bond
?-1,6-glycosidic bond
?-1,4-glycosidic bond
Cellulose is a polysaccharide made of ?-D-glucose units linked by ?-1,4-glycosidic bonds. This straight linkage allows extensive hydrogen bonding between chains, forming strong microfibrils. Humans lack the enzyme cellulase needed to break ?-1,4 bonds, making cellulose indigestible. https://en.wikipedia.org/wiki/Cellulose
Which amino acid acts as the nucleophile in the catalytic triad of serine proteases?
Histidine
Aspartate
Cysteine
Serine
Serine proteases use a catalytic triad composed of serine, histidine, and aspartate residues in the active site. The serine hydroxyl group acts as a nucleophile, attacking the carbonyl carbon of the peptide bond. This mechanism is essential for proteolysis in digestion and blood clotting. https://en.wikipedia.org/wiki/Serine_protease
Which molecule is a positive allosteric activator of pyruvate kinase in glycolysis?
Alanine
Fructose-1,6-bisphosphate
ATP
NADH
Allosteric regulators bind to sites other than the active site to modulate enzyme activity. Fructose-1,6-bisphosphate acts as a positive allosteric activator of pyruvate kinase in glycolysis, enhancing its catalytic efficiency. This feed-forward activation helps coordinate energy production pathways. https://en.wikipedia.org/wiki/Pyruvate_kinase#Regulation
Which interaction is the primary driver of a protein's tertiary structure?
Ionic bonds between charged side chains
Disulfide bridges
Hydrogen bonds between backbone atoms
Hydrophobic interactions among nonpolar side chains
The tertiary structure of a protein is its overall three-dimensional shape, primarily stabilized by hydrophobic interactions among nonpolar side chains. Additionally, ionic bonds, hydrogen bonds, and disulfide bridges contribute to the final folded form. Proper tertiary structure is critical for protein function and specificity. https://en.wikipedia.org/wiki/Protein_folding
In non-competitive enzyme inhibition, what is the effect on Km and Vmax?
Vmax decreases, Km increases
Vmax remains unchanged, Km decreases
Vmax decreases, Km remains unchanged
Vmax remains unchanged, Km increases
In non-competitive inhibition, inhibitors bind to an allosteric site rather than the active site. This binding reduces the total number of active enzyme molecules, lowering Vmax. Km remains unchanged because the affinity of the remaining active enzymes for substrate does not change. https://en.wikipedia.org/wiki/Enzyme_inhibitor#Non-competitive_inhibition
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Study Outcomes

  1. Understand Biomolecule Categories -

    Grasp the classification of the four major biomolecules and explain which group enzymes that speed up reactions belong to in a biomolecules test context.

  2. Classify Enzyme Functions -

    Recognize the characteristics of enzymes in a biochemistry enzymes test and determine how they accelerate biochemical reactions.

  3. Distinguish Carbohydrates, Lipids & Proteins -

    Differentiate these biomolecules by their structures and roles, preparing you for any biomolecules exam question.

  4. Apply Knowledge to Quiz Scenarios -

    Tackle enzymes quiz questions with confidence by applying principles of enzyme activity and specificity.

  5. Analyze Molecular Structures -

    Identify key structural features of biomolecules and predict how these features influence their functions in living systems.

  6. Evaluate Biomolecular Examples -

    Assess real-world examples of carbohydrates, lipids, proteins, and enzymes to reinforce learning and test readiness.

Cheat Sheet

  1. Enzyme Classification & Specificity -

    Enzymes which can speed up reactions belong in the biological catalyst category and are classified into six main groups by the IUBMB: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. A handy mnemonic "O-T-H-L-I-Lyases" helps you recall the order, and consulting official IUBMB resources (iubmb.org) ensures accurate enzyme class definitions. Mastering this classification is crucial for any biomolecules test or biochemistry enzymes test.

  2. Carbohydrate Structure & Glycosidic Bonds -

    Monosaccharides like glucose (C₆H₝₂O₆) can cyclize into alpha or beta anomers, and they link via glycosidic bonds (e.g., α-1,4 in maltose, β-1,4 in cellobiose) to form polysaccharides. Remember "Alpha straight chains, Beta bent bridges" as a mnemonic to distinguish bond orientation, a tip endorsed by many university biochemistry curricula (see PubChem entries on carbohydrates).

  3. Lipid Classification & Functions -

    Lipids include fatty acids, triacylglycerols, phospholipids, and steroids, each serving roles from energy storage to membrane structure and signaling. Use the mnemonic "FATS" (Fats store energy, Act as membranes, Thermal insulation, Steroids as hormones) referenced in the Lipid Metabolism section of Lehninger Principles to lock in these functions.

  4. Amino Acids & Protein Structures -

    Amino acids link via peptide bonds in dehydration reactions to build proteins with hierarchical structures: primary, secondary (α-helix/β-sheet), tertiary, and quaternary (e.g., hemoglobin). To memorize essential amino acids, recall "PVT TIM HALL," a classic student mnemonic found in many biochemistry exam prep guides.

  5. Enzyme Kinetics & Michaelis-Menten -

    The Michaelis-Menten equation (v = (Vmax·[S])/(Km + [S])) describes how reaction velocity depends on substrate concentration, with Km equal to the [S] at half Vmax. Visualize a Lineweaver-Burk double reciprocal plot to linearize data - "Y-intercept is 1/Vmax, X-intercept is -1/Km" - a strategy commonly taught in NCBI tutorials on enzyme kinetics.

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