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GATE General Biochemistry & Metabolism: practice questions

GATE — Life Sciences (XL), Section U Food Technology · India · IITs and IISc on rotation (2026: IIT Guwahati)

Original practice questions written to the published syllabus · not past papers
10worked here, free
36written to this exam in this subject
8syllabus units

What this subject covers

The structure of biomolecules and the metabolic pathways that turn food into energy and body tissue. Food chemistry (phase 2) describes how these molecules behave in a food; this subject explains how they behave in the body and in living raw materials such as respiring fruit and post-mortem muscle.

In the exams: ICAR AIEEA-PG Code 18 Unit I (metabolism of carbohydrates, lipids and protein; BV and PER)

Where the 36 questions fall

How our questions for GATE spread across the units of General Biochemistry & Metabolism. Difficulty: 10 easy, 23 medium, 3 hard.

Nucleic acids, replication, transcription and translation8
Enzymes: classification, mechanism, Michaelis-Menten kinetics and inhibition6
Biochemical laboratory techniques: centrifugation, electrophoresis and spectrophotometry6
Bioenergetics, ATP and the electron transport chain5
Carbohydrate metabolism: glycolysis, TCA cycle, gluconeogenesis and glycogen4
Biomolecules: carbohydrates, amino acids, proteins, lipids and nucleic acids3
Lipid metabolism: beta-oxidation and fatty-acid synthesis3
Protein and amino-acid metabolism and the urea cycle1

10 practice questions, worked

Choose an answer, then open the working. Each explanation says why the right answer is right and why the others are not.

1 · Biomolecules: carbohydrates, amino acids, proteins, lipids and nucleic acids · medium

Which level of protein structure is held mainly by hydrogen bonds between backbone C=O and N–H groups?

  1. Peptide bonds of the chain
  2. Secondary structure
  3. Quaternary structure
  4. Primary structure
Answer and working

B. Secondary structure

α-Helices and β-sheets are stabilised by hydrogen bonds between backbone carbonyl and amide groups. Primary structure is the covalent sequence; quaternary structure is the association of subunits through side-chain interactions.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

2 · Enzymes: classification, mechanism, Michaelis-Menten kinetics and inhibition · medium

A competitive inhibitor is added to an enzyme assay. What happens to the apparent Km and Vmax?

  1. Both Km and Vmax increase
  2. Km increases; Vmax is unchanged
  3. Km is unchanged; Vmax decreases
  4. Both Km and Vmax decrease
Answer and working

B. Km increases; Vmax is unchanged

A competitive inhibitor competes for the active site; enough substrate can outcompete it, so Vmax is reached but more substrate is needed (higher apparent Km). Unchanged Km with lower Vmax is pure non-competitive inhibition; both falling is uncompetitive.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

3 · Bioenergetics, ATP and the electron transport chain · medium

Using modern P/O ratios, how many ATP are formed when one NADH from the mitochondrial matrix is oxidised by the electron transport chain?

  1. Exactly 3
  2. About 1.5
  3. About 2.5
  4. Exactly 4
Answer and working

C. About 2.5

About 10 protons are pumped per NADH and about 4 are needed per ATP (including transport), giving about 2.5 ATP. 1.5 is the value for FADH₂; 3 is the older integral value.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

4 · Bioenergetics, ATP and the electron transport chain · easy

According to the chemiosmotic theory, what directly drives ATP synthesis in mitochondria?

  1. The flow of protons back through ATP synthase
  2. The reduction of oxygen inside ATP synthase
  3. The hydrolysis of GTP in the TCA cycle
  4. The direct transfer of electrons from NADH to ADP
Answer and working

A. The flow of protons back through ATP synthase

Electron transport pumps protons out; their return through the F₀F₁ ATP synthase drives its rotation and ATP formation. Electrons never reach ADP, GTP is a substrate-level product, and oxygen is reduced at complex IV.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

5 · Carbohydrate metabolism: glycolysis, TCA cycle, gluconeogenesis and glycogen · easy

What is the net yield of glycolysis per molecule of glucose?

  1. 36 ATP
  2. 2 ATP and 4 NADH
  3. 4 ATP and 2 NADH
  4. 2 ATP and 2 NADH
Answer and working

D. 2 ATP and 2 NADH

Four ATP are made, but two are invested, leaving net 2 ATP, plus 2 NADH from glyceraldehyde 3-phosphate dehydrogenase. 4 ATP is the gross figure; 36 ATP is an older figure for complete aerobic oxidation.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

6 · Carbohydrate metabolism: glycolysis, TCA cycle, gluconeogenesis and glycogen · medium

How many NADH, FADH₂ and GTP are produced per acetyl-CoA oxidised in the TCA cycle?

  1. 2 NADH, 2 FADH₂, 1 GTP
  2. 3 NADH, 1 FADH₂, 1 GTP
  3. 1 NADH, 1 FADH₂, 3 GTP
  4. 3 NADH, 2 FADH₂, 2 GTP
Answer and working

B. 3 NADH, 1 FADH₂, 1 GTP

Isocitrate, α-ketoglutarate and malate dehydrogenases give 3 NADH; succinate dehydrogenase gives 1 FADH₂; succinyl-CoA synthetase gives 1 GTP (or ATP). The other combinations do not match the cycle's dehydrogenases.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

7 · Protein and amino-acid metabolism and the urea cycle · medium

In the urea cycle, where do the two nitrogen atoms of urea come from?

  1. Both from free ammonia
  2. Both from glutamine
  3. One from arginine and one from ornithine
  4. One from free ammonia and one from aspartate
Answer and working

D. One from free ammonia and one from aspartate

Carbamoyl phosphate brings one nitrogen from NH₃ (via carbamoyl phosphate synthetase I) and argininosuccinate synthetase adds the second from aspartate. Ornithine is the carrier and is regenerated, so it contributes no nitrogen to urea.

Further reading: Lehninger Principles of Biochemistry; FAO Food and Nutrition Paper 92 (2013)

8 · Nucleic acids, replication, transcription and translation · easy

A double-stranded DNA contains 20% adenine. What percentage is guanine?

  1. 40%
  2. 60%
  3. 30%
  4. 20%
Answer and working

C. 30%

By Chargaff's rules, A = T = 20%, so A + T = 40% and G + C = 60%, giving G = 30%. 20% assumes all bases are equal; 40% gives G = A + T; 60% gives G + C together.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

9 · Nucleic acids, replication, transcription and translation · medium

Which DNA sample has the highest melting temperature?

  1. One with 50% G + C
  2. One with 30% G + C
  3. One with 70% A + T
  4. One with 70% G + C
Answer and working

D. One with 70% G + C

G-C pairs have three hydrogen bonds and stronger stacking than A-T pairs, so DNA richer in G + C needs more heat to separate its strands. 70% A + T is the same as 30% G + C.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

10 · Nucleic acids, replication, transcription and translation · medium

Which statement about eukaryotic messenger RNA processing is correct?

  1. It is capped, polyadenylated and spliced to remove introns
  2. Processing occurs on the ribosome during translation
  3. Bacterial mRNAs undergo the same splicing as eukaryotic mRNAs
  4. Exons are removed and introns are joined to form the mature mRNA
Answer and working

A. It is capped, polyadenylated and spliced to remove introns

The primary transcript is capped, polyadenylated and spliced (introns out, exons joined) in the nucleus before export. Bacteria generally lack introns and translate mRNA as it is being transcribed.

Further reading: Lehninger Principles of Biochemistry; Berg et al., Biochemistry

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General Biochemistry & MetabolismThe full study manual, free GATEFormat, sections and how it has changed

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General Biochemistry & Metabolism for other exams

ICAR AIEEA-PG / PGS · IndiaICAR AICE-JRF/SRF · India

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