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BIO NMDCAT

1785 questions found

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📁 ACELLULAR LIFR 20 📁 AIDS and HIV Infection 50 📁 and nerve impulse Reflexes and reflex arc 0 📁 Arthritis 0 📁 axon 0 📁 BIOENERGETICS 0 📁 Biological Importance of Water 95 📁 BIOLOGICAL MOLECULES 126 📁 Biotechnology 0 📁 Biotechnology and Health Care 0 📁 Blood Vessels 0 📁 Brain 25 📁 Carbohydrates 100 📁 Cardiac cycle and phases of Heartbeat 0 📁 cell body 0 📁 cell membrane 70 📁 CELL STRUCTURE & FUNCTION 100 📁 Chromosomes 76 📁 Circulation 0 📁 Concept of Evolution 50 📁 Conjugated molecules 100 📁 COORDINATION & CONTROL NERVOUS & CHEMICAL COORDINATION 0 📁 Cytoplasmic Organelles 75 📁 Darwinism 50 📁 dendrites 0 📁 DIVERSITY AMONG ANTMALS (THE KTNGDOM ANIMALIA) 0 📁 ENZYMES 108 📁 EVOLUTION 0 📁 Factors that Affect the Rate of Enzyme Reactions 60 📁 Form and Function in Plants 0 📁 Gene linkage and crossing over 0 📁 Homeostasis (kidney specifically) 0 📁 Homeostasis Mainly Kidney Portion nmdcat etea 0 📁 Human Heart 0 📁 Human Reproductive system 0 📁 Human Reproductive system-Menstrual cycle 0 📁 Human skeleton 0 📁 INHERITANCE 0 📁 Inhibitors 40 📁 Joints 0 📁 Lamarckism 50 📁 Lipids 45 📁 lmmunity 0 📁 Lymphatic system 0 📁 Mendel's laws of Inheritance 0 📁 Menstrual cycle 0 📁 Mode of Enzyme Action 60 📁 Muscle contraction 0 📁 Muscles 0 📁 myelin sheath 0 📁 Neurons 41 📁 PROKARYOTES (KTNGDOM MONERA) 0 📁 Prokaryotic and Eukaryotic cell 0 📁 Proteins 95 📁 Receptors 40 📁 REPRODUCTION 0 📁 Respiration 15 📁 Respiratory system 0 📁 Ribonucleic acid (RNA) 100 📁 Sexually transmitted diseases 50 📁 Skeletal muscles 0 📁 Specific Defense Mechanism 0 📁 Structure of DNA 98 📁 SUPPORT & MOVEMENT 0 📁 Viruses 46 📁 X-linked Recessive inheritance 0

Practice Questions

The primary function of an isoenzyme, such as lactate dehydrogenase (LDH), in a physiological context is to

A. Catalyze the same reaction but under different kinetic properties or regulatory conditions in different tissues
B. Bind to the same substrate to form different products depending on the organ
C. Act as a competitive inhibitor for the original enzyme
D. Combine several different metabolic pathways into a single rate-limiting step

Isoenzymes are multiple forms of an enzyme that catalyze the same reaction but differ in kinetic properties, allowing for tissue-specific metabolic tailoring.

nmdcat.online BIO NMDCAT
Jul 11, 2026

Many coenzymes are vitamin derivatives, such as pyridoxal phosphate (vitamin B6) which is required for aminotransferases.

nmdcat.online BIO NMDCAT
Jul 11, 2026

During an enzymatic reaction, the formation of an enzyme-substrate complex is primarily driven by

A. Covalent bonds formed at the catalytic site
B. Multiple weak interactions like hydrogen bonding and hydrophobic effects
C. The enzyme's ability to increase molecular collision frequency
D. Irreversible binding that ensures the substrate is fully processed

Substrate binding is mediated by multiple weak, non-covalent forces which are reversible, essential for both binding and product release.

nmdcat.online BIO NMDCAT
Jul 11, 2026

A coenzyme is a non-protein organic molecule that binds transiently to an apoenzyme, allowing it to be separated by dialysis, unlike a prosthetic group.

nmdcat.online BIO NMDCAT
Jul 11, 2026

The model of enzyme action that proposes the active site is flexible and molds itself around the substrate is the

A. Lock and Key model
B. Fluid Mosaic model
C. Induced Fit model
D. Template model

The Induced Fit model states the active site is not rigid; substrate binding induces a conformational change that properly positions catalytic groups for optimized catalysis.

nmdcat.online BIO NMDCAT
Jul 11, 2026

A graph of reaction rate versus substrate concentration for an enzyme-catalyzed reaction shows a hyperbolic curve because

A. Enzyme molecules become denatured at high substrate concentrations
B. Substrate molecules inhibit the reaction after a certain point
C. The enzyme becomes saturated, and all active sites are occupied
D. The activation energy increases exponentially with substrate concentration

At high substrate concentrations, all enzyme active sites are occupied. The reaction velocity reaches a maximum (Vmax), and further substrate addition cannot increase the rate.

nmdcat.online BIO NMDCAT
Jul 11, 2026

In the context of enzyme kinetics, the Michaelis constant (Km) is numerically equal to the

A. Maximum velocity the enzyme can achieve
B. Substrate concentration at which the reaction velocity is half of Vmax
C. Enzyme concentration required for half-maximal activity
D. Turnover number of the enzyme

Km is a measure of an enzyme's affinity for its substrate, defined as the substrate concentration at which the reaction rate is one-half of the maximum velocity (Vmax).

nmdcat.online BIO NMDCAT
Jul 11, 2026

In living organisms, the most fundamental role of an enzyme is to

A. Provide energy for a nonspontaneous reaction
B. Shift the equilibrium towards product formation
C. Increase the reaction rate by lowering activation energy
D. Alter the standard free energy change of a reaction

Enzymes are biological catalysts that accelerate reactions by decreasing the activation energy. They do not provide energy, alter the equilibrium constant, or change the free energy change (ΔG) of the overall reaction.

nmdcat.online BIO NMDCAT
Jul 11, 2026

The three-dimensional shape of an enzyme, crucial for its catalytic activity, is primarily maintained by

A. Peptide bonds linking amino acids in the polypeptide chain
B. Weak non-covalent interactions and disulfide bridges
C. Covalent cross-links formed between enzyme and cofactor
D. Hydrophobic exclusion of water molecules from the active site

The tertiary structure of an enzyme, which dictates the shape of the active site, is stabilized by hydrogen bonds, ionic interactions, hydrophobic interactions, van der Waals forces, and covalent disulfide bonds.

nmdcat.online BIO NMDCAT
Jul 11, 2026

A prosthetic group is a non-protein unit that is covalently or very tightly bound to an apoenzyme, making it a permanent part of the functional holoenzyme.

nmdcat.online BIO NMDCAT
Jul 11, 2026

Regarding the active site of an enzyme, the most accurate description is that it

A. Is a rigid, lock-like structure that perfectly fits the substrate
B. Consists of the entire three-dimensional structure of the protein
C. Is a flexible, three-dimensional cleft that binds and transforms the substrate
D. Functions independently of any non-amino acid components in the holoenzyme

The active site is a specific, flexible 3D pocket formed by a few amino acids that binds the substrate and catalyzes its conversion to product via weak interactions.

nmdcat.online BIO NMDCAT
Jul 11, 2026

The catalytic efficiency of an enzyme is best explained by the fact that it

A. Increases the kinetic energy of the substrate molecules
B. Provides a surface with specific chemical groups that reduce activation energy
C. Bends the substrate molecule until it breaks apart into products
D. Is completely consumed and regenerated after each catalytic cycle

Enzymes lower activation energy by providing an alternative reaction pathway where specific R-groups orient and stress substrates, stabilizing the transition state.

nmdcat.online BIO NMDCAT
Jul 11, 2026

Which proteins would you find on the surface of the cell membrane?

A. Integral
B. Peripheral
C. Channel
D. Transmembrane

Peripheral proteins sit on the outside (or inside) surface of the bilayer.

nmdcat.online BIO NMDCAT
Jul 8, 2026

The concentration gradient drives:

A. Active transport
B. Facilitated diffusion
C. Simple diffusion
D. Both B and C

Both facilitated and simple diffusion are passive processes driven by concentration gradients.

nmdcat.online BIO NMDCAT
Jul 8, 2026

Which molecule’s structure is a four-ring steroid?

A. Phospholipid
B. Cholesterol
C. Glycoprotein
D. Fatty acid

Cholesterol is a steroid, characterized by its four-ring hydrocarbon structure.

nmdcat.online BIO NMDCAT
Jul 8, 2026

What is the main purpose of “cell-cell recognition”?

A. Nutrient absorption
B. Immune response
C. Energy production
D. Waste removal

Immune cells use recognition markers to identify infected or foreign cells (e.g., pathogens).

nmdcat.online BIO NMDCAT
Jul 8, 2026

Why is the cell membrane described as “living”?

A. It produces DNA
B. It maintains its integrity/homeostasis
C. It is rigid
D. It does not move

Its ability to regulate its own composition and environment is a fundamental property of a living membrane.

nmdcat.online BIO NMDCAT
Jul 8, 2026

Which process is known as ‘cell drinking’?

A. Phagocytosis
B. Pinocytosis
C. Exocytosis
D. Diffusion

Pinocytosis is a type of endocytosis where the membrane invaginates to take in fluid.

nmdcat.online BIO NMDCAT
Jul 8, 2026

Which of the following is a function of the cell membrane?

A. Cell-cell recognition
B. ATP production
C. Protein synthesis
D. DNA replication

The cell membrane's surface markers are crucial for identifying "self" vs "non-self" cells.

nmdcat.online BIO NMDCAT
Jul 8, 2026
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