In enzymatic reactions, the molecule that results after the enzyme acts on a substrate is called the:
Reactant
Intermediate
Product
Effector
An enzyme composed of both a protein and a non-protein component is referred to as a:
Simple Enzyme
Apoenzyme
Conjugated Enzyme
Coenzyme
The inactive protein portion of an enzyme that requires a cofactor to function is the:
Holoenzyme
Apoenzyme
Zymogen
Isoenzyme
The non-protein component necessary for enzyme activity is called the:
Cofactor
Prosthetic group
Coenzyme
Apoenzyme
The enzyme that catalyzes the breakdown of urea into ammonia and carbon dioxide is:
Cellulase
Urease
Sucrase
Lipase
Enzymes possessing multiple subunits and both catalytic and regulatory binding sites are termed:
Holoenzyme
Allosteric Enzyme
Isoenzyme
Zymogen
The enzyme responsible for milk coagulation by acting on casein is:
Amylase
Rennin
Pepsin
Lactase
Enzymes that consist solely of protein, with no non-protein component, are called:
Simple Enzyme
Conjugated Enzyme
Apoenzyme
Metalloenzyme
The enzyme model that proposes enzyme flexibility allowing the active site to adjust to the substrate’s shape is known as the:
Lock-and-key model
Induced Fit Model
Complementary Model
Adaptive site model
Enzymes that have tightly bound metal ions (e.g., Zn²⁺, Fe²⁺) essential for catalytic activity are classified as:
Coenzyme
Metalloenzyme
Isoenzyme
Simple Enzyme
Menadione is also known as:
Vitamin E
Vitamin K
Vitamin D
Vitamin F
The “Chick Anti-Dermatitis Factor” is another name for which vitamin?
Nicacin
Riboflavin
Pantothenic acid
Pyridoxine
The active coenzyme form of Vitamin B1 (Thiamine) is:
Thiamine Pyrophosphate
Flavin mononucleotide
Pyridoxal phosphate
Coenzyme A
The active form of Pantothenic acid involved in acyl-transfer reactions is:
Coenzyme A
Thiamine Pyrophosphate
Biocytin
Folic Acid
A deficiency of a water-soluble antioxidant vitamin resulting in gum bleeding, poor collagen synthesis, and slow wound healing leads to:
Rickets
Pellagra
Scruvy
Beriberi
Enzymes that catalyze dehydration or decarboxylation reactions are classified as:
Lyase
Hydrolase
Oxidoreductase
Ligase
Enzymes that catalyze oxidation–reduction reactions (e.g., A + B + O₂ → C + H₂O) belong to:
Isomerase
Ligase
Oxidoreductase
Transferase
Mutases, which shift functional groups within the same molecule, are examples of:
Transferase
Isomerase
Lyases
Ligase
Synthetases, which form bonds between molecules using ATP, belong to the class of:
Ligases
Transferase
Lyase
Hydroalse
Dehydrogenases, which remove hydrogen atoms from substrates, are classified as:
Hydrolase
Lyase
Oxidoreductase
Isomerase
Enzymes that catalyze the transfer of amino groups between substrates are:
Transferase
Hydrolase
Ligase
Lyase
Enzymes that catalyze hydrolytic cleavage of bonds (A + H₂O → B + C) belong to:
Lyase
Isomerase
Hydrolase
Ligase
Enzymes that catalyze the breakdown of a compound into smaller ones without water are:
Ligase
Lyase
Oxidoreductase
Transferase
Enzymes that rearrange atoms within a molecule to form its isomeric counterpart are:
Isomerase
Hydrolase
Transferase
Lyase
Enzymes that catalyze the joining of two substrates with ATP involvement are:
Ligase
Transferase
Oxidoreductase
Isomerase