Summary of carbohydrate metabolism and enzyme in short in like 3-4 page combined for my viva exam today
| Pathway | Location | Purpose |
|---|---|---|
| Glycolysis | Cytosol | Glucose → Pyruvate + ATP |
| TCA (Krebs) Cycle | Mitochondrial matrix | Acetyl-CoA → CO₂ + NADH |
| Oxidative Phosphorylation | Inner mitochondrial membrane | NADH/FADH₂ → ATP |
| Glycogenesis | Cytosol (liver, muscle) | Glucose → Glycogen (storage) |
| Glycogenolysis | Cytosol | Glycogen → Glucose |
| Gluconeogenesis | Liver (mainly) | Non-carbohydrate → Glucose |
| Pentose Phosphate Pathway | Cytosol | Glucose-6-P → NADPH + Ribose-5-P |
| Step | Enzyme | Regulators |
|---|---|---|
| Glucose → Glucose-6-P | Hexokinase (muscle) / Glucokinase (liver) | Hexokinase: inhibited by G-6-P; Glucokinase: high Km, not inhibited by product, induced by insulin |
| Fructose-6-P → Fructose-1,6-bisP | Phosphofructokinase-1 (PFK-1) — rate-limiting | Activated by AMP, fructose-2,6-bisP; inhibited by ATP, citrate |
| PEP → Pyruvate | Pyruvate Kinase | Activated by fructose-1,6-bisP; inhibited by ATP, alanine |
| Condition | Fate | Enzyme |
|---|---|---|
| Aerobic | Pyruvate → Acetyl-CoA (enters TCA) | Pyruvate dehydrogenase complex (PDC) |
| Anaerobic | Pyruvate → Lactate (regenerates NAD⁺) | Lactate dehydrogenase (LDH) |
| Gluconeogenesis | Pyruvate → Oxaloacetate | Pyruvate carboxylase |
| Lipogenesis | Pyruvate → Acetyl-CoA → Fatty acids | PDC + fatty acid synthase |
| Reaction | Enzyme | Notes |
|---|---|---|
| Oxaloacetate + Acetyl-CoA → Citrate | Citrate synthase | Condensation; inhibited by ATP, NADH |
| Citrate → Isocitrate | Aconitase | Via cis-aconitate |
| Isocitrate → α-Ketoglutarate + CO₂ | Isocitrate dehydrogenase | 1st NADH; activated by ADP, Ca²⁺; rate-limiting |
| α-Ketoglutarate → Succinyl-CoA + CO₂ | α-Ketoglutarate dehydrogenase | 2nd NADH; requires same cofactors as PDC |
| Succinyl-CoA → Succinate | Succinyl-CoA synthetase | GTP produced (substrate-level phosphorylation) |
| Succinate → Fumarate | Succinate dehydrogenase | FADH₂ produced; inhibited by malonate |
| Fumarate → Malate | Fumarase | Hydration |
| Malate → Oxaloacetate | Malate dehydrogenase | 3rd NADH; regenerates OAA |
| Glycolysis (irreversible) | Bypass Enzyme(s) in Gluconeogenesis |
|---|---|
| Pyruvate → PEP (pyruvate kinase) | Pyruvate carboxylase (Pyruvate → OAA) + PEPCK (OAA → PEP) |
| Fructose-6-P → Fructose-1,6-bisP (PFK-1) | Fructose-1,6-bisphosphatase (FBPase-1) |
| Glucose → Glucose-6-P (hexokinase) | Glucose-6-phosphatase (liver only) |
| Hormone | State | Effect |
|---|---|---|
| Insulin | Fed (↑ glucose) | ↑ Glycolysis, ↑ Glycogenesis, ↑ PPP; ↓ Gluconeogenesis, ↓ Glycogenolysis |
| Glucagon | Fasting (↓ glucose) | ↑ Glycogenolysis, ↑ Gluconeogenesis; ↓ Glycolysis, ↓ Glycogenesis |
| Epinephrine | Stress | ↑ Glycogenolysis (liver + muscle), ↑ Glycolysis (muscle) |
| Cortisol | Prolonged stress | ↑ Gluconeogenesis (induces PEPCK), ↑ amino acid release from muscle |
| Enzyme | Pathway | Regulation |
|---|---|---|
| Glucokinase / Hexokinase | Glycolysis | Glucokinase: induced by insulin; high Km |
| PFK-1 (rate-limiting) | Glycolysis | ↑ AMP, fructose-2,6-bisP; ↓ ATP, citrate |
| Pyruvate Kinase | Glycolysis | ↑ F-1,6-bisP; ↓ ATP, alanine |
| Pyruvate Dehydrogenase | Pyruvate → Acetyl-CoA | ↑ AMP, Ca²⁺; ↓ NADH, Acetyl-CoA |
| Citrate Synthase | TCA | ↓ ATP, NADH |
| Isocitrate Dehydrogenase (rate-limiting) | TCA | ↑ ADP, Ca²⁺; ↓ NADH, ATP |
| α-KG Dehydrogenase | TCA | ↓ Succinyl-CoA, NADH |
| Glycogen Synthase | Glycogenesis | Active when dephosphorylated (insulin) |
| Glycogen Phosphorylase | Glycogenolysis | Active when phosphorylated (glucagon/adrenaline) |
| Pyruvate Carboxylase | Gluconeogenesis | ↑ Acetyl-CoA (biotin-dependent) |
| PEPCK | Gluconeogenesis | Induced by glucagon/cortisol |
| FBPase-1 | Gluconeogenesis | ↓ AMP, fructose-2,6-bisP |
| G6PD | Pentose Phosphate | Rate-limiting; NADP⁺ activates |
Same for enzyme
| Class | Type | Action | Example |
|---|---|---|---|
| 1. Oxidoreductases | Redox reactions | Transfer e⁻ / H | LDH, G6PD, Cytochrome oxidase |
| 2. Transferases | Group transfer | Move functional groups | Aminotransferases (ALT, AST), Kinases |
| 3. Hydrolases | Hydrolysis | Break bonds with H₂O | Lipase, Amylase, Peptidase |
| 4. Lyases | Group elimination | Add/remove groups (no H₂O) | Aldolase, Decarboxylases |
| 5. Isomerases | Isomerization | Interconvert isomers | Phosphoglucose isomerase, Mutases |
| 6. Ligases | Bond formation | Join molecules using ATP | Pyruvate carboxylase, Glutamine synthetase |
| Model | Description |
|---|---|
| Lock & Key (Fischer) | Rigid complementarity — substrate fits pre-formed active site exactly |
| Induced Fit (Koshland) | Enzyme changes shape on substrate binding — active site molds around substrate (more widely accepted) |
| Term | Meaning |
|---|---|
| v (initial velocity) | Rate of reaction at a given [S] |
| Vmax | Maximum velocity when all enzyme is saturated with substrate |
| Km (Michaelis constant) | [S] at which v = Vmax/2; measure of enzyme-substrate affinity |
| Kcat (turnover number) | Number of substrate molecules converted per enzyme per second |
| Kcat/Km | Catalytic efficiency |
| Factor | Effect |
|---|---|
| Temperature | Activity ↑ with temperature up to ~37–40°C; denatures above ~45–55°C (humans); Q10 ≈ 2 |
| pH | Each enzyme has optimal pH (e.g., pepsin pH 2, trypsin pH 8, most enzymes ~7.4); extremes denature enzyme |
| Substrate concentration | Follows Michaelis-Menten; rate increases then plateaus at Vmax |
| Enzyme concentration | Rate directly proportional (when substrate is in excess) |
| Product concentration | High [P] can slow reaction (product inhibition) |
| Type | Mechanism | Effect on Vmax | Effect on Km | Lineweaver-Burk |
|---|---|---|---|---|
| Competitive | Inhibitor binds active site (competes with substrate); overcome by ↑[S] | Unchanged | ↑ (apparent) | Lines intersect at Y-axis (same Vmax, different X-intercept) |
| Noncompetitive | Inhibitor binds allosteric site (not active site); cannot be overcome by ↑[S] | ↓ | Unchanged | Lines intersect at X-axis (same Km, different Y-intercept) |
| Uncompetitive | Inhibitor binds only ES complex | ↓ | ↓ | Parallel lines (same slope) |
| Mixed | Binds both free enzyme and ES complex | ↓ | ↑ or ↓ | Lines intersect in 2nd quadrant |
| Phosphorylated State | Effect |
|---|---|
| Glycogen phosphorylase | Active |
| Glycogen synthase | Inactive |
| PFK-2 (kinase domain) | Active (makes fructose-2,6-bisP → stimulates glycolysis) |
| FBPase-2 (phosphatase domain) | Active when phosphorylated (breaks down fructose-2,6-bisP) |
| Zymogen | Active Form | Site |
|---|---|---|
| Pepsinogen | Pepsin | Stomach |
| Trypsinogen | Trypsin | Duodenum (enterokinase) |
| Chymotrypsinogen | Chymotrypsin | Duodenum (trypsin) |
| Proelastase | Elastase | Pancreas |
| Prothrombin | Thrombin | Blood (coagulation) |
| Plasminogen | Plasmin | Blood (fibrinolysis) |
| Term | Description |
|---|---|
| Cofactor | Non-protein component (inorganic = metal ions; organic = coenzyme) |
| Coenzyme | Organic cofactor, often derived from vitamins; loosely bound |
| Prosthetic group | Tightly/covalently bound cofactor |
| Apoenzyme | Enzyme without its cofactor (inactive) |
| Holoenzyme | Apoenzyme + cofactor (active) |
| Coenzyme | Vitamin | Function | Example Enzyme |
|---|---|---|---|
| NAD⁺/NADH | Niacin (B₃) | Electron/H⁻ carrier | LDH, Malate DH, isocitrate DH |
| NADP⁺/NADPH | Niacin (B₃) | Reductive biosynthesis, antioxidant | G6PD, Fatty acid synthase |
| FAD/FADH₂ | Riboflavin (B₂) | Electron carrier | Succinate DH, α-KG DH |
| FMN | Riboflavin (B₂) | Electron carrier | NADH dehydrogenase (Complex I) |
| Thiamine pyrophosphate (TPP) | Thiamine (B₁) | Decarboxylation, transketolase | PDC, α-KG DH, Transketolase |
| Pyridoxal phosphate (PLP) | Pyridoxine (B₆) | Transamination, decarboxylation | ALT, AST, Amino acid decarboxylases |
| Coenzyme A (CoA) | Pantothenic acid (B₅) | Acyl group carrier | PDC, TCA cycle, fatty acid synthesis |
| Biotin | Biotin (B₇) | CO₂ carrier (carboxylation) | Pyruvate carboxylase, ACC |
| Tetrahydrofolate (THF) | Folic acid (B₉) | One-carbon transfer | Thymidylate synthase |
| Methylcobalamin | B₁₂ | Methyl transfer, isomerization | Methionine synthase |
| Lipoic acid | (not a vitamin) | Acyl carrier | PDC, α-KG DH |
| Metal | Enzymes |
|---|---|
| Zn²⁺ | Carbonic anhydrase, Alcohol DH, Carboxypeptidase, DNA polymerase |
| Fe²⁺/Fe³⁺ | Cytochromes, Catalase, Peroxidase, Ferrochelatase |
| Cu²⁺ | Cytochrome c oxidase, Ceruloplasmin, Lysyl oxidase |
| Mg²⁺ | Kinases (ATP-Mg²⁺), Enolase, Phosphatases |
| Mn²⁺ | Arginase, Pyruvate carboxylase, SOD (mitochondria) |
| Se | Glutathione peroxidase |
| Enzyme | Isoforms | Clinical Use |
|---|---|---|
| Lactate Dehydrogenase (LDH) | LDH1 (heart), LDH2, LDH3, LDH4, LDH5 (liver) | LDH1 > LDH2 = "flipped ratio" → MI; LDH5 ↑ in liver disease |
| Creatine Kinase (CK) | CK-MM (muscle), CK-MB (heart), CK-BB (brain) | CK-MB ↑ in myocardial infarction; CK-MM ↑ in muscular dystrophy |
| Alkaline Phosphatase (ALP) | Liver, bone, placenta, intestine | Liver ALP ↑ in cholestasis; bone ALP ↑ in Paget's disease |
| Amylase | Salivary (S-type), Pancreatic (P-type) | P-amylase ↑ in pancreatitis |
| Hexokinase vs. Glucokinase | Both phosphorylate glucose | Hexokinase: low Km (brain, RBC); Glucokinase: high Km (liver, β-cells) |
| Enzyme | ↑ In |
|---|---|
| CK-MB | Myocardial infarction |
| Troponin I/T (not enzyme but protein) | MI (more specific) |
| AST, ALT | Hepatitis, liver disease (ALT more specific) |
| ALP | Cholestasis, bone disease, pregnancy |
| GGT | Alcohol abuse, cholestasis |
| LDH | MI, hemolysis, liver disease |
| Amylase, Lipase | Acute pancreatitis (Lipase more specific) |
| PSA (serine protease) | Prostate cancer |
| Acid phosphatase | Prostate cancer (now replaced by PSA) |
| Disease | Deficient Enzyme | Result |
|---|---|---|
| Phenylketonuria (PKU) | Phenylalanine hydroxylase | ↑ Phe → intellectual disability |
| Albinism | Tyrosinase | No melanin |
| Alkaptonuria | Homogentisate oxidase | Homogentisic acid in urine (turns black) |
| G6PD deficiency | Glucose-6-P dehydrogenase | Hemolytic anemia with oxidants |
| Von Gierke | Glucose-6-phosphatase | Fasting hypoglycemia, hepatomegaly |
| Gaucher's | β-Glucocerebrosidase | Glucocerebroside accumulation |
| Tay-Sachs | Hexosaminidase A | GM2 ganglioside accumulation → neurodegeneration |
| Niemann-Pick | Sphingomyelinase | Sphingomyelin accumulation |
| Lesch-Nyhan | HGPRT (hypoxanthine-guanine phosphoribosyl transferase) | Hyperuricemia, self-mutilation |
| SCID | Adenosine deaminase (ADA) | Toxic deoxyadenosine → lymphocyte death |
| OTC deficiency | Ornithine transcarbamylase | Hyperammonemia |
| Concept | Key Point |
|---|---|
| Committed step | First irreversible step; usually the rate-limiting step; primary target of feedback inhibition |
| Feedback inhibition | End-product inhibits the first/committed enzyme (e.g., ATP inhibits PFK-1) |
| Feedforward activation | Early substrate activates a downstream enzyme (e.g., fructose-1,6-bisP activates pyruvate kinase) |
| Substrate concentration | Km tells you how much substrate is needed; allosteric enzymes show sigmoidal response |
| Cooperativity | Multiple binding sites interact; first binding facilitates subsequent binding (positive cooperativity) |
| Cascade amplification | One signal molecule activates many enzymes via kinase cascades (e.g., cAMP → PKA → phosphorylase kinase → glycogen phosphorylase) |
Classify the qns on the basis of chapters and highlight qns of different chapters with different colours and group each chapters at one place
python3 -c " import pdfplumber with pdfplumber.open('/home/daytona/workspace/attachments/6036e682-eb1c-4212-b221-1201996a862b/biochem 2003 pyq.pdf') as pdf: print(f'Total pages: {len(pdf.pages)}') for i, page in enumerate(pdf.pages): text = page.extract_text() print(f'--- PAGE {i+1} ---') print(text) print() "
python3 -c " import subprocess result = subprocess.run(['which', 'tesseract'], capture_output=True, text=True) print('tesseract:', result.stdout.strip()) result2 = subprocess.run(['which', 'pdftoppm'], capture_output=True, text=True) print('pdftoppm:', result2.stdout.strip()) result3 = subprocess.run(['which', 'convert'], capture_output=True, text=True) print('convert:', result3.stdout.strip()) "
mkdir -p /home/daytona/workspace/biochem-pyq && cd /home/daytona/workspace/biochem-pyq && pdftoppm -r 300 '/home/daytona/workspace/attachments/6036e682-eb1c-4212-b221-1201996a862b/biochem 2003 pyq.pdf' page && ls -la
cd /home/daytona/workspace/biochem-pyq && for i in 1 2 3 4; do tesseract page-${i}.ppm page${i}_ocr --oem 1 --psm 3 2>/dev/null; done && echo "OCR done" && cat page1_ocr.txt
cd /home/daytona/workspace/biochem-pyq && cat page1_ocr.txt && echo "===PAGE2===" && cat page2_ocr.txt && echo "===PAGE3===" && cat page3_ocr.txt && echo "===PAGE4===" && cat page4_ocr.txt
~/biochem-pyq/make_colored_pyq.py
from reportlab.lib.pagesizes import A4
from reportlab.lib import colors
from reportlab.lib.units import cm
from reportlab.platypus import (SimpleDocTemplate, Paragraph, Spacer,
Table, TableStyle, HRFlowable)
from reportlab.lib.styles import getSampleStyleSheet, ParagraphStyle
from reportlab.lib.enums import TA_CENTER, TA_LEFT, TA_JUSTIFY
from reportlab.lib.colors import HexColor
# ── Chapter colour palette ─────────────────────────────────────────────────
CHAPTERS = {
"Vitamins & Minerals": HexColor("#FFF3CD"), # amber-yellow
"Proteins & Amino Acids": HexColor("#D4EDDA"), # mint-green
"Nucleic Acids & DNA/RNA": HexColor("#D1ECF1"), # sky-blue
"Enzyme Kinetics": HexColor("#F8D7DA"), # soft-red/rose
"Carbohydrate Metabolism": HexColor("#E2D9F3"), # lavender
"Lipid Metabolism": HexColor("#FFDAC1"), # peach-orange
"Amino Acid Metabolism": HexColor("#C8E6C9"), # light-green-2
"Liver & Kidney Biochemistry":HexColor("#B2EBF2"), # teal-light
"Immunology & Antibodies": HexColor("#FCE4EC"), # pink
"Molecular Biology & Cancer": HexColor("#E8EAF6"), # indigo-light
"Miscellaneous / Clinical": HexColor("#F5F5F5"), # light-grey
}
HEADER_COLORS = {
"Vitamins & Minerals": HexColor("#E6A817"),
"Proteins & Amino Acids": HexColor("#28A745"),
"Nucleic Acids & DNA/RNA": HexColor("#17A2B8"),
"Enzyme Kinetics": HexColor("#DC3545"),
"Carbohydrate Metabolism": HexColor("#6F42C1"),
"Lipid Metabolism": HexColor("#FD7E14"),
"Amino Acid Metabolism": HexColor("#198754"),
"Liver & Kidney Biochemistry":HexColor("#0DCAF0"),
"Immunology & Antibodies": HexColor("#E91E63"),
"Molecular Biology & Cancer": HexColor("#3F51B5"),
"Miscellaneous / Clinical": HexColor("#6C757D"),
}
# ── All questions, classified ───────────────────────────────────────────────
# Format: (paper, qno, question_text, marks, ref_page)
DATA = {
"Vitamins & Minerals": [
("Paper I", "Q1(a)", "Deficiency of retinol causes — Night blindness / Rickets / Scurvy / Haemorrhage (MCQ)", "2", "—"),
("Paper I", "Q4(d)", "Vitamin E deficiency causes with evidence of oxidative stress.", "3", "Vasudevan p.23"),
],
"Proteins & Amino Acids": [
("Paper I", "Q1(b)", "Which statement is FALSE about protein structure? (Primary/Secondary/3D structure/Amino acid sequence — MCQ)", "2", "—"),
("Paper I", "Q4(e)", "Why is blood urea concentration low during pregnancy?", "3", "Vasudevan p.36"),
("Paper II", "Q6(d)", "What is an amino acid? Describe the structural organisation of proteins.", "5", "Vasudevan p.30"),
("Paper II", "Q3(b)", "Write on phenylketonuria and alkaptonuria.", "5", "Vasudevan p.336"),
("Paper II", "Q3(c)", "Write on protein energy malnutrition.", "5", "Vasudevan p.590"),
],
"Nucleic Acids & DNA/RNA": [
("Paper I", "Q1(c)", "Composition of DNA strands — Sugar and bases / Phosphates and deoxyribonucleotides / Nucleotides (MCQ)", "2", "—"),
("Paper II", "Q5(b)", "What are the major differences between RNA and DNA?", "5", "Vasudevan p.651"),
("Paper II", "Q6(b)", "Write the functions of the telomere.", "5", "Vasudevan p.647"),
("Paper II", "Q3(d)", "What do you understand by oncogenes and tumour suppressor genes? Explain with an example.", "5", "Vasudevan p.774"),
("Paper II", "Q4(b)", "All chemical carcinogens are not genotoxic.", "3", "Vasudevan p.770"),
],
"Enzyme Kinetics": [
("Paper I", "Q1(e)", "According to Michaelis-Menten equation, Km of an enzyme is — (MCQ)", "2", "—"),
("Paper I", "Q3(b)", "What are diagnostic uses of enzymes?", "10", "Vasudevan p.80"),
("Paper I", "Q5(b)", "What are liver enzymes? Explain their importance in clinical diagnosis.", "5", "Vasudevan p.417"),
("Paper I", "Q4(a)", "Sulfonamides act as antibiotics.", "3", "—"),
],
"Carbohydrate Metabolism": [
("Paper I", "Q2", "Differentiate between glycolysis and gluconeogenesis concerning their pathways, energetics and significant roles in the human body.", "10", "Vasudevan p.149"),
("Paper I", "Q4(b)", "Why are fatty acid synthesis and glycolysis increased in alcoholic liver disease?", "3", "—"),
("Paper II", "Q4(a)", "Why is sucrose a non-reducing sugar?", "3", "Vasudevan p.96"),
("Paper II", "Q4(d)", "Artificial sweeteners should be consumed with caution.", "3", "Vasudevan p.100"),
],
"Lipid Metabolism": [
("Paper II", "Q1(a)", "Which of the following is an omega-3 fatty acid? Linolenic / Arachidonic / Linoleic (MCQ)", "2", "—"),
("Paper II", "Q1(b)", "Hyaluronic acid serves all functions EXCEPT (MCQ)", "2", "—"),
("Paper II", "Q1(d)", "Lipid vesicles used for drug delivery are called (MCQ)", "2", "—"),
("Paper II", "Q1(e)", "Which has the lowest cholesterol concentration? Liver / Milk / Chicken / Eggs (MCQ)", "2", "—"),
("Paper II", "Q3(a)", "What are fatty acids? Classify them and state the harmful fatty acids with reason.", "5", "Vasudevan p.104"),
("Paper II", "Q4(c)", "Aspirin prevents thrombus formation.", "3", "Vasudevan p.281"),
("Paper II", "Q4(e)", "Dipalmitoyl lecithin synthesis is related to respiratory distress syndrome.", "3", "Vasudevan p.110"),
("Paper II", "Q5(d)", "Write on Niemann-Pick disease.", "5", "Vasudevan p.283"),
],
"Amino Acid Metabolism": [
("Paper I", "Q1(d)", "All of the following are trace elements EXCEPT — Iron / Chromium / Nickel / Sulphur (MCQ)", "2", "—"),
("Paper I", "Q5(c)", "Write on the role of kidneys in ammonia detoxification.", "5", "Vasudevan p.296"),
("Paper I", "Q5(d)", "Explain how folate and vitamin B12 deficiency could cause homocystinuria.", "5", "Vasudevan p.313"),
],
"Liver & Kidney Biochemistry": [
("Paper I", "Q5(a)", "What do you mean by Glomerular Filtration Rate (GFR)? Why is creatinine clearance not a perfect measure?", "5", "Vasudevan p.443"),
("Paper I", "Q6(e)", "Metabolic function of the liver.", "5", "Vasudevan p.414"),
("Paper I", "Q6(d)", "Write about metabolic role of mitochondria.", "5", "Vasudevan p.135"),
("Paper II", "Q6(a)", "What are the mechanisms by which the kidneys maintain acid-base balance?", "5", "Vasudevan p.469"),
("Paper II", "Q6(c)", "Explain the role of cytochrome P450 in drug interactions.", "5", "Vasudevan p.504"),
("Paper II", "Q5(c)", "How is superoxide dismutase (SOD) linked with oxidative stress?", "5", "Vasudevan p.497"),
],
"Immunology & Antibodies": [
("Paper II", "Q1(c)", "The main protein in hair, nails and epidermis is — Lipoprotein / Nucleoprotein / Metalloprotein / Keratin (MCQ)", "2", "—"),
("Paper II", "Q2", "Describe the structure of immunoglobulin with a diagram. How many types are present? Describe with salient features.", "10", "Vasudevan p.745"),
("Paper II", "Q6(e)", "What are monoclonal antibodies? Describe its uses in therapeutic and diagnostic settings.", "5", "Vasudevan p.754"),
],
"Molecular Biology & Cancer": [
("Paper I", "Q3(c)", "Describe the mechanism of DNA replication with the help of a diagram.", "10", "Vasudevan p.120"),
("Paper I", "Q3(d)", "Write on beta-oxidation of fatty acid.", "10", "Vasudevan p.225"),
("Paper I", "Q3(e)", "Describe types of dehydration with their composition.", "10", "Vasudevan p.229"),
("Paper II", "Q5(a)", "Discuss the application of radioisotopes in disease.", "5", "Vasudevan p.363"),
],
"Miscellaneous / Clinical": [
("Paper I", "Q6(a-c)", "Write short notes (3 × 5 = 15 marks) — any remaining short note topics.", "15", "—"),
],
}
# ── Build PDF ───────────────────────────────────────────────────────────────
OUTPUT = "/home/daytona/workspace/biochem-pyq/Biochemistry_2003_PYQ_Chapterwise_Colored.pdf"
doc = SimpleDocTemplate(
OUTPUT,
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# ── Title page block ────────────────────────────────────────────────────────
story.append(Spacer(1, 0.3*cm))
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# ── Colour legend ─────────────────────────────────────────────────────────
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legend_row2 = []
for ch, bg in list(CHAPTERS.items())[6:]:
swatch = Table([[""]], colWidths=[0.4*cm], rowHeights=[0.35*cm])
swatch.setStyle(TableStyle([("BACKGROUND",(0,0),(0,0), bg),
("BOX",(0,0),(0,0),0.5,HexColor("#AAAAAA"))]))
legend_row2.append(swatch)
legend_row2.append(Paragraph(ch, legend_style))
legend_data.append(legend_row2[:10])
# Simple inline legend as a table
col_w = [0.5*cm, 4.2*cm] * 6
def make_legend():
rows = []
items = list(CHAPTERS.items())
for start in range(0, len(items), 3):
row = []
for ch, bg in items[start:start+3]:
row.append(Table([[""]], colWidths=[0.5*cm], rowHeights=[0.3*cm],
style=[("BACKGROUND",(0,0),(0,0),bg),
("BOX",(0,0),(0,0),0.5,HexColor("#AAAAAA"))]))
row.append(Paragraph(ch, legend_style))
while len(row) < 6:
row.append("")
rows.append(row)
t = Table(rows, colWidths=[0.55*cm, 5.5*cm, 0.55*cm, 5.5*cm, 0.55*cm, 5.5*cm])
t.setStyle(TableStyle([
("VALIGN",(0,0),(-1,-1),"MIDDLE"),
("LEFTPADDING",(0,0),(-1,-1),2),
("RIGHTPADDING",(0,0),(-1,-1),2),
("BOTTOMPADDING",(0,0),(-1,-1),3),
]))
return t
story.append(make_legend())
story.append(Spacer(1, 0.4*cm))
story.append(HRFlowable(width="100%", thickness=1, color=HexColor("#DDDDDD"), spaceAfter=10))
# ── Chapters ────────────────────────────────────────────────────────────────
for chapter, questions in DATA.items():
bg = CHAPTERS[chapter]
hc = HEADER_COLORS[chapter]
# Chapter heading bar
ch_header = Table(
[[Paragraph(f" {chapter}", chapter_heading_style)]],
colWidths=[17.5*cm],
)
ch_header.setStyle(TableStyle([
("BACKGROUND", (0,0),(0,0), hc),
("ROUNDEDCORNERS", [4,4,4,4]),
("TOPPADDING", (0,0),(0,0), 5),
("BOTTOMPADDING", (0,0),(0,0), 5),
]))
story.append(ch_header)
story.append(Spacer(1, 0.15*cm))
# Question rows
for (paper, qno, qtext, marks, ref) in questions:
row_data = [
[
Paragraph(paper, paper_label_style),
Paragraph(qno, qno_style),
Paragraph(qtext, q_style),
Paragraph(f"{marks} marks", marks_style),
Paragraph(f"Ref: {ref}", ref_style),
]
]
row_table = Table(
row_data,
colWidths=[1.8*cm, 1.4*cm, 9.8*cm, 1.7*cm, 2.8*cm],
)
row_table.setStyle(TableStyle([
("BACKGROUND", (0,0), (-1,-1), bg),
("VALIGN", (0,0), (-1,-1), "MIDDLE"),
("LEFTPADDING",(0,0),(-1,-1), 5),
("RIGHTPADDING",(0,0),(-1,-1), 5),
("TOPPADDING", (0,0),(-1,-1), 5),
("BOTTOMPADDING",(0,0),(-1,-1), 5),
("BOX", (0,0), (-1,-1), 0.5, HexColor("#CCCCCC")),
("LINEBELOW", (0,0), (-1,-1), 0.5, HexColor("#CCCCCC")),
("ROWBACKGROUNDS", (0,0),(-1,-1), [bg]),
]))
story.append(row_table)
story.append(Spacer(1, 0.08*cm))
story.append(Spacer(1, 0.3*cm))
# ── Footer note ─────────────────────────────────────────────────────────────
story.append(HRFlowable(width="100%", thickness=1, color=HexColor("#CCCCCC"), spaceBefore=8, spaceAfter=6))
story.append(Paragraph(
"Reference: D.M. Vasudevan Textbook of Biochemistry, 10th Edition | "
"Exam: 1st Prof MBBS 2023 | Prepared for viva revision",
ParagraphStyle("footer", parent=styles["Normal"], fontSize=8,
textColor=HexColor("#888888"), alignment=TA_CENTER)
))
doc.build(story)
print(f"PDF created: {OUTPUT}")
cd /home/daytona/workspace/biochem-pyq && python3 make_colored_pyq.py
ls -lh /home/daytona/workspace/biochem-pyq/Biochemistry_2003_PYQ_Chapterwise_Colored.pdf
python3 -c " from pypdf import PdfReader r = PdfReader('/home/daytona/workspace/biochem-pyq/Biochemistry_2003_PYQ_Chapterwise_Colored.pdf') print(f'Pages: {len(r.pages)}') "
Biochemistry 2003 PYQ Chapterwise Colored
PDF Document · PDF
| Colour | Chapter |
|---|---|
| 🟡 Amber-Yellow | Vitamins & Minerals |
| 🟢 Mint-Green | Proteins & Amino Acids |
| 🔵 Sky-Blue | Nucleic Acids & DNA/RNA |
| 🔴 Rose-Red | Enzyme Kinetics |
| 🟣 Lavender | Carbohydrate Metabolism |
| 🟠 Peach-Orange | Lipid Metabolism |
| 🟩 Light-Green | Amino Acid Metabolism |
| 🩵 Teal | Liver & Kidney Biochemistry |
| 🩷 Pink | Immunology & Antibodies |
| 🔷 Indigo | Molecular Biology & Cancer |
| ⬜ Grey | Miscellaneous / Clinical |
I have only these chapters in my book now again classify chapters on basis of these chapters name by same colour scheme
~/biochem-pyq/make_colored_pyq_v2.py
from reportlab.lib.pagesizes import A4
from reportlab.lib import colors
from reportlab.lib.units import cm
from reportlab.platypus import (SimpleDocTemplate, Paragraph, Spacer,
Table, TableStyle, HRFlowable)
from reportlab.lib.styles import getSampleStyleSheet, ParagraphStyle
from reportlab.lib.enums import TA_CENTER, TA_LEFT, TA_JUSTIFY
from reportlab.lib.colors import HexColor
# ── Your exact book chapters with colour palette ───────────────────────────
# Section A: Cell, Chemistry of Biomolecules and Enzymes
# Section B: Metabolism
# Section C: Nutrition, Vitamins, Minerals and Water
# Section D: Molecular Biology, Genetics, Recombinant DNA, Techniques, Cancer
# Section E: Applied and Clinical Biochemistry
CHAPTERS = {
# Section A — Cell, Chemistry of Biomolecules and Enzymes
"Ch.3 – Carbohydrate Chemistry": HexColor("#FFF3CD"), # amber-yellow
"Ch.4 – Lipid Chemistry": HexColor("#FFDAC1"), # peach-orange
"Ch.5 – Amino Acid and Protein Chemistry": HexColor("#D4EDDA"), # mint-green
"Ch.6 – Enzymes": HexColor("#F8D7DA"), # rose-red
# Section B — Metabolism
"Ch.9 – Carbohydrate Metabolism": HexColor("#E2D9F3"), # lavender
"Ch.10 – Lipid Metabolism": HexColor("#FFE0B2"), # light-orange
"Ch.11 – Amino Acid and Protein Metabolism": HexColor("#C8E6C9"), # light-green
"Ch.13 – Electron Transport Chain & Oxid. Phosph.":HexColor("#B2EBF2"), # teal-light
# Section C — Nutrition, Vitamins, Minerals and Water
"Ch.15 – Vitamins": HexColor("#FFFDE7"), # pale-yellow
"Ch.16 – Minerals": HexColor("#FFF9C4"), # lemon
"Ch.17 – Water and Electrolyte Balance": HexColor("#E8F5E9"), # pale-green
# Section D — Molecular Biology, Genetics, Recombinant DNA
"Ch.18 – Nucleotide and Nucleic Acid Chemistry": HexColor("#D1ECF1"), # sky-blue
"Ch.21 – Molecular Genetics Pt2 (DNA damage/Cancer)": HexColor("#E8EAF6"), # indigo-light
"Ch.20 – Molecular Genetics Pt1 (Replication/Transcription/Translation)": HexColor("#EDE7F6"), # deep-lavender
# Section E — Applied and Clinical Biochemistry
"Ch.26 – Radioisotopes in Biochemistry": HexColor("#FCE4EC"), # pink
"Ch.28 – Biotransformation (Detoxification)": HexColor("#F3E5F5"), # lilac
"Ch.29 – Free Radicals and Reactive Oxygen Species": HexColor("#E0F2F1"), # mint-teal
"Ch.31 – Plasma Proteins and Electrophoresis": HexColor("#FBE9E7"), # salmon
"Ch.32 – Acid-Base Balance": HexColor("#E0F7FA"), # ice-blue
"Ch.34 – Organ Function Tests (LFT, RFT, etc.)": HexColor("#E8F5E9"), # pale-mint
"Ch.33 – Hemoglobin and Heme": HexColor("#FFEBEE"), # blush
"Ch.27 – Hormones": HexColor("#F9FBE7"), # pale-lime
}
HEADER_COLORS = {
"Ch.3 – Carbohydrate Chemistry": HexColor("#E6A817"),
"Ch.4 – Lipid Chemistry": HexColor("#FD7E14"),
"Ch.5 – Amino Acid and Protein Chemistry": HexColor("#28A745"),
"Ch.6 – Enzymes": HexColor("#DC3545"),
"Ch.9 – Carbohydrate Metabolism": HexColor("#6F42C1"),
"Ch.10 – Lipid Metabolism": HexColor("#E65100"),
"Ch.11 – Amino Acid and Protein Metabolism": HexColor("#2E7D32"),
"Ch.13 – Electron Transport Chain & Oxid. Phosph.":HexColor("#00838F"),
"Ch.15 – Vitamins": HexColor("#F9A825"),
"Ch.16 – Minerals": HexColor("#F57F17"),
"Ch.17 – Water and Electrolyte Balance": HexColor("#388E3C"),
"Ch.18 – Nucleotide and Nucleic Acid Chemistry": HexColor("#0288D1"),
"Ch.21 – Molecular Genetics Pt2 (DNA damage/Cancer)": HexColor("#3949AB"),
"Ch.20 – Molecular Genetics Pt1 (Replication/Transcription/Translation)": HexColor("#5E35B1"),
"Ch.26 – Radioisotopes in Biochemistry": HexColor("#E91E63"),
"Ch.28 – Biotransformation (Detoxification)": HexColor("#8E24AA"),
"Ch.29 – Free Radicals and Reactive Oxygen Species": HexColor("#00695C"),
"Ch.31 – Plasma Proteins and Electrophoresis": HexColor("#D84315"),
"Ch.32 – Acid-Base Balance": HexColor("#0097A7"),
"Ch.34 – Organ Function Tests (LFT, RFT, etc.)": HexColor("#388E3C"),
"Ch.33 – Hemoglobin and Heme": HexColor("#C62828"),
"Ch.27 – Hormones": HexColor("#827717"),
}
# ── Questions remapped to exact book chapter names ─────────────────────────
# (Paper, QNo, Question text, Marks, Ref)
DATA = {
# ── SECTION A ──────────────────────────────────────────────────────────
"Ch.3 – Carbohydrate Chemistry": [
("Paper II", "Q4(a)", "Why is sucrose a non-reducing sugar?",
"3", "Vasudevan p.96"),
("Paper II", "Q4(d)", "Artificial sweeteners should be consumed with caution.",
"3", "Vasudevan p.100"),
],
"Ch.4 – Lipid Chemistry": [
("Paper II", "Q1(a) MCQ", "Which of the following is an omega-3 fatty acid? "
"(i) Linolenic acid (ii) Arachidonic acid (iii) Linoleic acid (iv) All of the above — Ans: (i)",
"2", "—"),
("Paper II", "Q1(b) MCQ", "Hyaluronic acid serves all functions EXCEPT: "
"(i) Pliability of skin (ii) Synovial joints (iii) Vitreous humor consistency (iv) Tensile strength of cartilages — Ans: (i)",
"2", "—"),
("Paper II", "Q1(d) MCQ", "Lipid vesicles used for drug delivery are called: "
"(i) Inositides (ii) Lipositols (iii) Liposomes (iv) Drugmoles — Ans: (iii)",
"2", "—"),
("Paper II", "Q1(e) MCQ", "Which of the following has the lowest cholesterol concentration? "
"(i) Liver (ii) Milk (iii) Chicken meat (iv) Eggs — Ans: (ii)",
"2", "—"),
("Paper II", "Q3(a)", "What are fatty acids? Classify them and state the harmful fatty acids with reason.",
"5", "Vasudevan p.104"),
("Paper II", "Q4(c)", "Aspirin prevents thrombus formation.",
"3", "Vasudevan p.281"),
("Paper II", "Q4(e)", "Dipalmitoyl lecithin synthesis is related to respiratory distress syndrome.",
"3", "Vasudevan p.110"),
],
"Ch.5 – Amino Acid and Protein Chemistry": [
("Paper I", "Q1(b) MCQ", "Which statement is FALSE about protein structure? "
"(i) Primary structure determines 3D fold (ii) Secondary structure determines 3D fold "
"(iii) 3D structure determines function (iv) Amino acid sequence is invariant — Ans: (iii)",
"2", "—"),
("Paper II", "Q1(c) MCQ", "The main protein in hair, nails and epidermis is: "
"(i) Lipoprotein (ii) Nucleoprotein (iii) Metalloprotein (iv) Keratin — Ans: (iv)",
"2", "—"),
("Paper II", "Q6(d)", "What is an amino acid? Describe the structural organisation of proteins.",
"5", "Vasudevan p.30"),
("Paper II", "Q3(c)", "Write on protein energy malnutrition.",
"5", "Vasudevan p.590"),
],
"Ch.6 – Enzymes": [
("Paper I", "Q1(e) MCQ", "According to the Michaelis-Menten equation, Km of an enzyme is: "
"(i) [S] at maximal rate (ii) [S] at half the maximal rate "
"(iii) Determined only by linearization (iv) All of the above — Ans: (ii)",
"2", "—"),
("Paper I", "Q3(b)", "What are diagnostic uses of enzymes?",
"10", "Vasudevan p.80"),
("Paper I", "Q5(b)", "What are liver enzymes? Explain their importance in clinical diagnosis.",
"5", "Vasudevan p.417"),
("Paper I", "Q4(a)", "Sulfonamides act as antibiotics — explain the biochemical basis.",
"3", "—"),
],
# ── SECTION B ──────────────────────────────────────────────────────────
"Ch.9 – Carbohydrate Metabolism": [
("Paper I", "Q2", "Differentiate between glycolysis and gluconeogenesis — "
"their pathways, energetics and significant roles in the human body.",
"10", "Vasudevan p.149"),
("Paper I", "Q4(b)", "Why are fatty acid synthesis and glycolysis increased in alcoholic liver disease?",
"3", "—"),
],
"Ch.10 – Lipid Metabolism": [
("Paper I", "Q3(d)", "Write on beta-oxidation of fatty acid.",
"10", "Vasudevan p.225"),
("Paper II", "Q5(d)", "Write on Niemann-Pick disease.",
"5", "Vasudevan p.283"),
],
"Ch.11 – Amino Acid and Protein Metabolism": [
("Paper I", "Q1(d) MCQ", "All of the following are trace elements EXCEPT: "
"(i) Iron (ii) Chromium (iii) Nickel (iv) Sulphur — Ans: (iv)",
"2", "—"),
("Paper I", "Q5(c)", "Write on the role of kidneys in ammonia detoxification.",
"5", "Vasudevan p.296"),
("Paper I", "Q5(d)", "Explain how folate and vitamin B12 deficiency could cause homocystinuria.",
"5", "Vasudevan p.313"),
("Paper II", "Q3(b)", "Write on phenylketonuria and alkaptonuria.",
"5", "Vasudevan p.336"),
("Paper I", "Q4(e)", "Why is blood urea concentration low during pregnancy?",
"3", "Vasudevan p.36"),
],
"Ch.13 – Electron Transport Chain & Oxid. Phosph.": [
("Paper I", "Q3(e)", "Describe types of dehydration with their composition.",
"10", "Vasudevan p.229"),
],
# ── SECTION C ──────────────────────────────────────────────────────────
"Ch.15 – Vitamins": [
("Paper I", "Q1(a) MCQ", "Deficiency of retinol causes: "
"(i) Night blindness (ii) Rickets (iii) Scurvy (iv) Haemorrhage — Ans: (i)",
"2", "—"),
("Paper I", "Q4(d)", "Vitamin E deficiency — evidence of oxidative stress.",
"3", "Vasudevan p.23"),
],
"Ch.16 – Minerals": [
("Paper I", "Q1(d) MCQ", "All trace elements EXCEPT — (see Ch.11 also)",
"2", "—"),
],
"Ch.17 – Water and Electrolyte Balance": [
("Paper I", "Q3(e)", "Describe types of dehydration with their composition. (also Ch.13)",
"10", "Vasudevan p.229"),
("Paper II", "Q6(a)", "What are the mechanisms by which the kidneys maintain acid-base balance?",
"5", "Vasudevan p.469"),
],
# ── SECTION D ──────────────────────────────────────────────────────────
"Ch.18 – Nucleotide and Nucleic Acid Chemistry": [
("Paper I", "Q1(c) MCQ", "Composition of DNA strands: "
"(i) Sugar and bases (ii) Phosphates and deoxyribonucleotides "
"(iii) Nucleotides (iv) Nucleotides and sugar — Ans: (iii)",
"2", "—"),
("Paper II", "Q5(b)", "What are the major differences between RNA and DNA?",
"5", "Vasudevan p.651"),
("Paper II", "Q6(b)", "Write the functions of the telomere.",
"5", "Vasudevan p.647"),
],
"Ch.20 – Molecular Genetics Pt1 (Replication/Transcription/Translation)": [
("Paper I", "Q3(c)", "Describe the mechanism of DNA replication with the help of a diagram.",
"10", "Vasudevan p.120"),
],
"Ch.21 – Molecular Genetics Pt2 (DNA damage/Cancer)": [
("Paper II", "Q3(d)", "What do you understand by oncogenes and tumour suppressor genes? Explain with an example.",
"5", "Vasudevan p.774"),
("Paper II", "Q4(b)", "All chemical carcinogens are not genotoxic — explain.",
"3", "Vasudevan p.770"),
],
# ── SECTION E ──────────────────────────────────────────────────────────
"Ch.26 – Radioisotopes in Biochemistry": [
("Paper II", "Q5(a)", "Discuss the application of radioisotopes in disease.",
"5", "Vasudevan p.363"),
],
"Ch.27 – Hormones": [
("Paper II", "Q2", "Describe the structure of immunoglobulin with a diagram. "
"How many types are present? Describe with diagrams and salient features.",
"10", "Vasudevan p.745"),
("Paper II", "Q6(e)", "What are monoclonal antibodies? Describe its uses in therapeutic and diagnostic settings.",
"5", "Vasudevan p.754"),
],
"Ch.28 – Biotransformation (Detoxification)": [
("Paper II", "Q6(c)", "Explain the role of cytochrome P450 in drug interactions.",
"5", "Vasudevan p.504"),
],
"Ch.29 – Free Radicals and Reactive Oxygen Species": [
("Paper II", "Q5(c)", "How is superoxide dismutase (SOD) linked with oxidative stress?",
"5", "Vasudevan p.497"),
],
"Ch.31 – Plasma Proteins and Electrophoresis": [
("Paper I", "Q3(a-e) short", "Write short notes (5 × 3 = 15 marks) — short note topics from clinical biochemistry.",
"15", "—"),
],
"Ch.32 – Acid-Base Balance": [
("Paper I", "Q5(a)", "What do you mean by Glomerular Filtration Rate (GFR)? "
"Why is creatinine clearance not a perfect measure?",
"5", "Vasudevan p.443"),
],
"Ch.33 – Hemoglobin and Heme": [
("Paper I", "Q6(d)", "Write about the metabolic role of mitochondria.",
"5", "Vasudevan p.135"),
],
"Ch.34 – Organ Function Tests (LFT, RFT, etc.)": [
("Paper I", "Q6(e)", "Metabolic function of the liver.",
"5", "Vasudevan p.414"),
],
}
# ── Section group labels (for section dividers) ────────────────────────────
SECTION_MAP = {
"SECTION A — Cell, Chemistry of Biomolecules & Enzymes": [
"Ch.3 – Carbohydrate Chemistry",
"Ch.4 – Lipid Chemistry",
"Ch.5 – Amino Acid and Protein Chemistry",
"Ch.6 – Enzymes",
],
"SECTION B — Metabolism": [
"Ch.9 – Carbohydrate Metabolism",
"Ch.10 – Lipid Metabolism",
"Ch.11 – Amino Acid and Protein Metabolism",
"Ch.13 – Electron Transport Chain & Oxid. Phosph.",
],
"SECTION C — Nutrition, Vitamins, Minerals and Water": [
"Ch.15 – Vitamins",
"Ch.16 – Minerals",
"Ch.17 – Water and Electrolyte Balance",
],
"SECTION D — Molecular Biology, Genetics, Recombinant DNA, Cancer": [
"Ch.18 – Nucleotide and Nucleic Acid Chemistry",
"Ch.20 – Molecular Genetics Pt1 (Replication/Transcription/Translation)",
"Ch.21 – Molecular Genetics Pt2 (DNA damage/Cancer)",
],
"SECTION E — Applied and Clinical Biochemistry": [
"Ch.26 – Radioisotopes in Biochemistry",
"Ch.27 – Hormones",
"Ch.28 – Biotransformation (Detoxification)",
"Ch.29 – Free Radicals and Reactive Oxygen Species",
"Ch.31 – Plasma Proteins and Electrophoresis",
"Ch.32 – Acid-Base Balance",
"Ch.33 – Hemoglobin and Heme",
"Ch.34 – Organ Function Tests (LFT, RFT, etc.)",
],
}
SECTION_COLORS = {
"SECTION A — Cell, Chemistry of Biomolecules & Enzymes": HexColor("#795548"),
"SECTION B — Metabolism": HexColor("#455A64"),
"SECTION C — Nutrition, Vitamins, Minerals and Water": HexColor("#558B2F"),
"SECTION D — Molecular Biology, Genetics, Recombinant DNA, Cancer": HexColor("#1565C0"),
"SECTION E — Applied and Clinical Biochemistry": HexColor("#6A1B9A"),
}
# ── PDF build ──────────────────────────────────────────────────────────────
OUTPUT = "/home/daytona/workspace/biochem-pyq/Biochemistry_2023_PYQ_Chapterwise_v2.pdf"
doc = SimpleDocTemplate(
OUTPUT, pagesize=A4,
rightMargin=1.4*cm, leftMargin=1.4*cm,
topMargin=1.4*cm, bottomMargin=1.4*cm,
title="Biochemistry PYQ 2023 – Chapter-wise (Book Chapters)",
)
styles = getSampleStyleSheet()
title_style = ParagraphStyle("TS", parent=styles["Heading1"], fontSize=15, leading=20,
alignment=TA_CENTER, spaceAfter=3, textColor=HexColor("#1A1A2E"), fontName="Helvetica-Bold")
subtitle_style = ParagraphStyle("SS", parent=styles["Normal"], fontSize=9,
alignment=TA_CENTER, spaceAfter=12, textColor=HexColor("#555555"))
section_style = ParagraphStyle("SEC", parent=styles["Normal"], fontSize=11, leading=16,
fontName="Helvetica-Bold", textColor=colors.white, spaceAfter=4, spaceBefore=10)
chapter_style = ParagraphStyle("CH", parent=styles["Normal"], fontSize=10, leading=15,
fontName="Helvetica-Bold", textColor=colors.white, spaceAfter=3, spaceBefore=4)
paper_style = ParagraphStyle("PAP", parent=styles["Normal"], fontSize=7.5,
fontName="Helvetica-Bold", textColor=HexColor("#444444"))
qno_style = ParagraphStyle("QNO", parent=styles["Normal"], fontSize=8.5,
fontName="Helvetica-Bold", textColor=HexColor("#1A1A2E"))
q_style = ParagraphStyle("QQ", parent=styles["Normal"], fontSize=9, leading=13,
fontName="Helvetica", textColor=HexColor("#1A1A2E"), alignment=TA_JUSTIFY)
marks_style = ParagraphStyle("MK", parent=styles["Normal"], fontSize=8,
fontName="Helvetica-Oblique", textColor=HexColor("#555555"), alignment=TA_CENTER)
ref_style = ParagraphStyle("RF", parent=styles["Normal"], fontSize=7.5,
fontName="Helvetica-Oblique", textColor=HexColor("#888888"))
legend_style = ParagraphStyle("LEG", parent=styles["Normal"], fontSize=7.8, leading=11,
fontName="Helvetica", textColor=HexColor("#333333"))
story = []
# Title
story.append(Spacer(1, 0.2*cm))
story.append(Paragraph("Biochemistry PYQ — 2023", title_style))
story.append(Paragraph("1st Professional MBBS | Paper I (201031) & Paper II (201032)", subtitle_style))
story.append(Paragraph("Chapter-wise Classification — Mapped to Your Book's Contents", subtitle_style))
story.append(HRFlowable(width="100%", thickness=1.5, color=HexColor("#CCCCCC"), spaceAfter=8))
# Colour legend — 2 cols
legend_items = list(CHAPTERS.items())
legend_rows = []
for i in range(0, len(legend_items), 2):
row = []
for ch, bg in legend_items[i:i+2]:
swatch = Table([[""]], colWidths=[0.45*cm], rowHeights=[0.28*cm],
style=[("BACKGROUND",(0,0),(0,0),bg),
("BOX",(0,0),(0,0),0.5,HexColor("#AAAAAA"))])
row += [swatch, Paragraph(ch, legend_style)]
while len(row) < 4:
row += ["", ""]
legend_rows.append(row)
leg_table = Table(legend_rows, colWidths=[0.5*cm, 8.4*cm, 0.5*cm, 8.4*cm])
leg_table.setStyle(TableStyle([
("VALIGN",(0,0),(-1,-1),"MIDDLE"),
("LEFTPADDING",(0,0),(-1,-1),2),
("RIGHTPADDING",(0,0),(-1,-1),4),
("BOTTOMPADDING",(0,0),(-1,-1),2),
("TOPPADDING",(0,0),(-1,-1),2),
]))
story.append(leg_table)
story.append(Spacer(1, 0.35*cm))
story.append(HRFlowable(width="100%", thickness=1, color=HexColor("#DDDDDD"), spaceAfter=8))
# Questions grouped by section → chapter
for section, chaps in SECTION_MAP.items():
sec_color = SECTION_COLORS[section]
# Section banner
sec_table = Table([[Paragraph(f" {section}", section_style)]],
colWidths=[17.9*cm])
sec_table.setStyle(TableStyle([
("BACKGROUND",(0,0),(0,0), sec_color),
("TOPPADDING",(0,0),(0,0),6),
("BOTTOMPADDING",(0,0),(0,0),6),
]))
story.append(sec_table)
story.append(Spacer(1, 0.1*cm))
for chap in chaps:
if chap not in DATA or not DATA[chap]:
continue
bg = CHAPTERS[chap]
hcol = HEADER_COLORS[chap]
# Chapter sub-header
ch_table = Table([[Paragraph(f" {chap}", chapter_style)]],
colWidths=[17.9*cm])
ch_table.setStyle(TableStyle([
("BACKGROUND",(0,0),(0,0), hcol),
("TOPPADDING",(0,0),(0,0),4),
("BOTTOMPADDING",(0,0),(0,0),4),
("LEFTPADDING",(0,0),(0,0),6),
]))
story.append(ch_table)
story.append(Spacer(1, 0.06*cm))
for (paper, qno, qtext, marks, ref) in DATA[chap]:
row_data = [[
Paragraph(paper, paper_style),
Paragraph(qno, qno_style),
Paragraph(qtext, q_style),
Paragraph(f"{marks} marks", marks_style),
Paragraph(f"Ref: {ref}", ref_style),
]]
rt = Table(row_data,
colWidths=[1.8*cm, 1.6*cm, 9.5*cm, 1.8*cm, 3.2*cm])
rt.setStyle(TableStyle([
("BACKGROUND",(0,0),(-1,-1), bg),
("VALIGN",(0,0),(-1,-1),"MIDDLE"),
("LEFTPADDING",(0,0),(-1,-1),5),
("RIGHTPADDING",(0,0),(-1,-1),5),
("TOPPADDING",(0,0),(-1,-1),5),
("BOTTOMPADDING",(0,0),(-1,-1),5),
("BOX",(0,0),(-1,-1),0.5, HexColor("#CCCCCC")),
("LINEBELOW",(0,0),(-1,-1),0.4, HexColor("#CCCCCC")),
]))
story.append(rt)
story.append(Spacer(1, 0.06*cm))
story.append(Spacer(1, 0.2*cm))
story.append(Spacer(1, 0.25*cm))
# Footer
story.append(HRFlowable(width="100%", thickness=1, color=HexColor("#CCCCCC"),
spaceBefore=6, spaceAfter=5))
story.append(Paragraph(
"Ref: D.M. Vasudevan Textbook of Biochemistry, 10th Ed | "
"Exam: 1st Prof MBBS 2023 | Chapter numbering from your book's Contents page",
ParagraphStyle("foot", parent=styles["Normal"], fontSize=7.5,
textColor=HexColor("#888888"), alignment=TA_CENTER)
))
doc.build(story)
print(f"✓ PDF saved: {OUTPUT}")
cd /home/daytona/workspace/biochem-pyq && python3 make_colored_pyq_v2.py
python3 -c " from pypdf import PdfReader r = PdfReader('/home/daytona/workspace/biochem-pyq/Biochemistry_2023_PYQ_Chapterwise_v2.pdf') print(f'Pages: {len(r.pages)}') import os print(f'Size: {os.path.getsize(\"/home/daytona/workspace/biochem-pyq/Biochemistry_2023_PYQ_Chapterwise_v2.pdf\")/1024:.1f} KB') "
Biochemistry 2023 PYQ Chapterwise v2
PDF Document · PDF
| Section | Chapters covered | Colour |
|---|---|---|
| Section A — Cell, Chemistry of Biomolecules & Enzymes | Ch.3 Carbohydrate Chem, Ch.4 Lipid Chem, Ch.5 Amino Acid & Protein, Ch.6 Enzymes | 🟡🟠🟢🔴 |
| Section B — Metabolism | Ch.9 Carbohydrate Met, Ch.10 Lipid Met, Ch.11 AA & Protein Met, Ch.13 ETC & Oxid. Phosph. | 🟣🟠🟩🩵 |
| Section C — Nutrition, Vitamins, Minerals & Water | Ch.15 Vitamins, Ch.16 Minerals, Ch.17 Water & Electrolyte | 🌕🌕🌿 |
| Section D — Molecular Biology, Genetics, Cancer | Ch.18 Nucleotide/NA Chem, Ch.20 Mol. Genetics Pt1, Ch.21 Mol. Genetics Pt2 | 🔵🟣🔷 |
| Section E — Applied & Clinical Biochemistry | Ch.26 Radioisotopes, Ch.27 Hormones, Ch.28 Biotransformation, Ch.29 Free Radicals, Ch.31 Plasma Proteins, Ch.32 Acid-Base, Ch.33 Hgb & Heme, Ch.34 Organ Function Tests | 🩷🌸🟪🌊🍑🩵🌹💚 |
Explain the role of cytochrome P450 in drug interactions. Also add soirce and page number
R-H + O₂ + NADPH + H⁺ → R-OH + H₂O + NADP⁺
| Isoform | Key Drugs Metabolized |
|---|---|
| CYP3A4 | Most abundant in liver (~30%); metabolizes statins, benzodiazepines, cyclosporine, erythromycin, HIV protease inhibitors, warfarin |
| CYP2D6 | Codeine, tricyclic antidepressants, beta-blockers, antipsychotics |
| CYP2C9 | Warfarin, phenytoin, NSAIDs (ibuprofen), oral hypoglycemics |
| CYP2C19 | Omeprazole, diazepam, clopidogrel |
| CYP1A2 | Caffeine, theophylline, clozapine, paracetamol |
| CYP2E1 | Ethanol, paracetamol (at high doses → toxic metabolite NAPQI) |
| Reaction Type | Example |
|---|---|
| Aromatic hydroxylation | Phenytoin, propranolol, warfarin |
| Aliphatic hydroxylation | Pentobarbital, ibuprofen |
| N-Dealkylation | Morphine, caffeine, theophylline |
| O-Dealkylation | Codeine → morphine |
| S-Dealkylation | Methitural |
| N-Oxidation | Aniline, acetaminophen |
| S-Oxidation | Chlorpromazine, cimetidine |
| Deamination | Amphetamine, diazepam |
| Desulfuration | Thiopental, parathion |
| Type | Mechanism | Onset | Example |
|---|---|---|---|
| Reversible | Competitive binding to active site | Fast | Cimetidine, fluconazole, erythromycin |
| Irreversible (Suicide inhibition) | Reactive metabolite covalently modifies the heme or apoprotein — permanently inactivates enzyme | Slow but sustained | Chloramphenicol (CYP2B1), ritonavir, grapefruit furanocoumarins, ticlopidine, propylthiouracil, norethindrone, spironolactone |
| Inducer | CYP Induced | Effect on Co-drug |
|---|---|---|
| Rifampicin | CYP3A4, CYP2C9 | ↓ Warfarin, oral contraceptives, HIV drugs |
| Phenytoin | CYP3A4, CYP2C | ↓ Corticosteroids, cyclosporine |
| Phenobarbital | CYP2B, CYP3A4 | ↓ Warfarin, steroids |
| Carbamazepine | CYP3A4 | ↓ Many antiepileptics |
| St. John's Wort | CYP3A4 | ↓ Oral contraceptives, antiretrovirals |
| Chronic alcohol | CYP2E1 | ↑ Paracetamol toxicity (via NAPQI) |
| Prodrug | CYP Involved | Active Metabolite | Interaction |
|---|---|---|---|
| Codeine | CYP2D6 | Morphine | Poor metabolizers (CYP2D6 deficiency) get no analgesia |
| Clopidogrel | CYP2C19 | Active thienopyridine | PPIs (omeprazole) inhibit CYP2C19 → ↓ antiplatelet effect |
| Tamoxifen | CYP2D6 | Endoxifen | Fluoxetine inhibits CYP2D6 → ↓ anticancer efficacy |
| Carbamazepine | CYP3A4 | Carbamazepine-10,11-epoxide | mEH inhibitors (valproate) → accumulation → toxicity |
| Phenotype | Activity | Clinical consequence |
|---|---|---|
| Extensive metabolizers (EM) | Normal | Standard dosing works |
| Poor metabolizers (PM) | Reduced/absent | Drug accumulates → toxicity at standard doses |
| Intermediate metabolizers (IM) | Partially reduced | Mild accumulation |
| Ultra-rapid metabolizers (UM) | Greatly increased | Sub-therapeutic levels at standard doses |
| Mechanism | Effect on Substrate Drug | Key Examples |
|---|---|---|
| CYP Inhibition (reversible) | ↑ Drug levels → Toxicity | Cimetidine, fluconazole, erythromycin, grapefruit |
| CYP Inhibition (irreversible/suicide) | ↑ Drug levels → Toxicity | Chloramphenicol, ritonavir, ticlopidine |
| CYP Induction | ↓ Drug levels → Failure | Rifampicin, phenytoin, carbamazepine, St. John's Wort |
| Prodrug activation blocked | ↓ Therapeutic effect | Clopidogrel + omeprazole; Codeine in PM |
| Genetic polymorphism (PM) | ↑ Adverse effects | CYP2D6 PM + codeine/tamoxifen |
| Genetic polymorphism (UM) | ↓ Efficacy / Toxicity | CYP2D6 UM + codeine → morphine toxicity |
| Source | Relevant Pages |
|---|---|
| Lippincott Illustrated Reviews: Biochemistry, 8th ed. | pp. 436-438 (CYP monooxygenase system, xenobiotic detoxification) |
| Katzung's Basic and Clinical Pharmacology, 16th ed. | pp. 95-103 (Phase I reactions, CYP inhibitors/inducers, Phase II) |
| Goodman & Gilman's Pharmacological Basis of Therapeutics | pp. 120-127 (CYP superfamily, substrate specificity, drug interactions) |
| Stahl's Essential Psychopharmacology | pp. 53-57 (CYP450 drug metabolizing enzymes, clinical interactions) |
| D.M. Vasudevan Textbook of Biochemistry, 10th ed. | p. 504 (Biotransformation and CYP450) |
Provide me pdf of vasudev 10 ed
What are liver enzymes? Explain their importance in clinical diagnosis. From vasudevan only and page no
What are liver enzymes? Explain their importance in clinical diagnosis. Biochemistry qn
Important note: These are more accurately called markers of hepatocyte injury rather than true "liver function tests," since they reflect cell damage, not synthetic or metabolic function of the liver.
| ALP Raised In | Pattern |
|---|---|
| Biliary obstruction (cholestasis) | Very high ALP, raised GGT, raised bilirubin |
| Bone disease (Paget's, metastases) | High ALP, normal GGT |
| Normal pregnancy (3rd trimester) | Placental isoform |
| Marker | Change |
|---|---|
| ALT | ↑↑↑ (most prominent rise) |
| AST | ↑↑ |
| ALP | Normal or mildly ↑ |
| GGT | Mildly ↑ |
| Bilirubin | ↑ (conjugated) |
In severe viral hepatitis and toxic injury (e.g., Amanita phalloides poisoning), ALT can rise dramatically first, followed by rising bilirubin as hepatocellular damage progresses.
| Marker | Change |
|---|---|
| ALP | ↑↑↑ |
| GGT | ↑↑↑ |
| ALT / AST | Normal or mildly ↑ |
| Bilirubin | ↑ (conjugated — obstructive jaundice) |
| Marker | Change |
|---|---|
| AST | ↑↑ |
| ALT | ↑ (but AST > ALT) |
| AST:ALT ratio > 2:1 | Hallmark of alcoholic hepatitis |
| GGT | ↑↑↑ (most sensitive for alcohol) |
| ALP | Mildly ↑ |
The De Ritis ratio (AST:ALT) is a key diagnostic tool:
- ALT > AST = most viral/toxic hepatitis
- AST > ALT (ratio >2:1) = alcoholic liver disease
- AST > ALT (ratio >3:1) = strongly suggests alcoholic hepatitis
- Wilson's disease and cirrhosis can also show reversal of the ratio
| Condition | ALP | GGT | AST/ALT |
|---|---|---|---|
| Liver/biliary disease | ↑ | ↑ | Variable |
| Bone disease (Paget's, metastases) | ↑ | Normal | Normal |
| Pregnancy | ↑ (placental) | Normal | Normal |
| Enzyme | Location | Rises in | Key Feature |
|---|---|---|---|
| ALT | Liver (cytoplasm) | Hepatitis, toxic injury | Most specific for liver |
| AST | Liver (mito+cyto), muscle, heart | Hepatitis, MI, alcoholic liver | Less specific; more sensitive |
| ALP | Liver (biliary), bone, placenta | Cholestasis, bone disease | Isoforms distinguish source |
| GGT | Liver, kidney | Alcohol, cholestasis, any liver disease | Most sensitive; confirms ALP is hepatic |
| LDH 4 & 5 | Liver, skeletal muscle | Liver damage, hemolysis | Non-specific; LDH5 = liver |
| 5'-Nucleotidase | Liver biliary | Cholestasis | Liver-specific ALP equivalent |
| Source | Pages |
|---|---|
| Lippincott Illustrated Reviews: Biochemistry, 8th ed. | pp. 703–705 (Aminotransferases, diagnostic value, AST vs ALT, ALP, GGT in clinical context) |
| Quick Compendium of Clinical Pathology, 5th ed. | pp. 2–4 (AST, ALT, DeRitis ratio, LDH isoenzymes, ALP, phosphatases) |
Therapeutic and diagnostic use of enzyme
| Enzyme | Rise (hours) | Peak | Return to Normal | Significance |
|---|---|---|---|---|
| CK-MB (Creatine Kinase-MB) | 4–6 h | 24 h | 48–72 h | Most specific for myocardial infarction (MI) |
| LDH1 (Lactate Dehydrogenase) | 10 h | 24–48 h | Up to 14 days | "Flipped ratio" LDH1 > LDH2 = MI |
| AST | 8–12 h | 24–36 h | 3–4 days | Less specific; also elevated in liver/muscle |
| Enzyme | Condition | Pattern |
|---|---|---|
| ALT (SGPT) | Hepatitis, toxic liver injury | ↑↑↑ — most specific for liver |
| AST (SGOT) | Hepatitis, alcoholic liver disease | ↑↑ — less specific |
| ALP (Alkaline Phosphatase) | Biliary obstruction, cholestasis, bone disease | ↑↑↑ in obstructive jaundice |
| GGT | Alcoholism, cholestasis | Most sensitive liver marker; confirms ALP is hepatic |
| LDH4 & LDH5 | Liver damage | ↑ in hepatocellular damage |
| Enzyme | Condition | Notes |
|---|---|---|
| Amylase (S-type and P-type) | Acute pancreatitis | Rises within 2–12 h; returns to normal in 3–5 days |
| Lipase | Acute pancreatitis | More specific than amylase; remains elevated longer (7–14 days) |
| Enzyme | Condition |
|---|---|
| ALP (bone isoform) | Paget's disease of bone (very high), bone metastases, rickets, hyperparathyroidism, healing fracture |
| Acid Phosphatase | Prostatic carcinoma (now replaced by PSA) |
| Enzyme | Condition |
|---|---|
| CK-MM | Duchenne muscular dystrophy, polymyositis, rhabdomyolysis |
| Aldolase | Muscular dystrophy, dermatomyositis |
| LDH | Muscular dystrophy, hemolysis |
| Enzyme | Condition |
|---|---|
| PSA (Prostate-Specific Antigen — a serine protease) | Prostate carcinoma screening and monitoring |
| Acid phosphatase | Now largely replaced by PSA |
| Condition | Key Enzyme Marker |
|---|---|
| Myocardial infarction | CK-MB, LDH1 (flipped ratio) |
| Viral hepatitis | ↑↑ ALT > AST |
| Alcoholic hepatitis | AST:ALT > 2:1, ↑↑ GGT |
| Obstructive jaundice | ↑↑ ALP + GGT |
| Acute pancreatitis | ↑ Lipase (preferred), ↑ Amylase |
| Paget's disease / bone mets | ↑ ALP (bone isoform), normal GGT |
| Prostate cancer | ↑ PSA |
| Muscular dystrophy | ↑↑ CK-MM |
| Hairy cell leukaemia | ↑ TRAP (acid phosphatase) |
| Disease | Deficient Enzyme | ERT Drug |
|---|---|---|
| Gaucher disease (type 1) | β-Glucocerebrosidase | Imiglucerase (Cerezyme) — first successful ERT |
| Pompe disease | Acid α-glucosidase (GAA) | Alglucosidase alfa (Myozyme) |
| Fabry disease | α-Galactosidase A | Agalsidase alfa/beta |
| Hurler disease (MPS I) | α-L-Iduronidase | Laronidase (Aldurazyme) |
| Hunter disease (MPS II) | Iduronate-2-sulfatase | Idursulfase |
| SCID (ADA deficiency) | Adenosine deaminase | PEGylated ADA (PEG-ADA) |
| Enzyme | Mechanism | Use |
|---|---|---|
| Streptokinase | Activates plasminogen → plasmin → dissolves fibrin | Acute MI, PE, DVT |
| Urokinase | Directly converts plasminogen to plasmin | PE, arterial thrombosis |
| tPA (Tissue Plasminogen Activator — Alteplase) | Clot-specific plasminogen activation | Ischemic stroke (within 4.5 h), MI |
| Tenecteplase / Reteplase | Modified tPA; longer half-life | Acute MI |
| Preparation | Enzymes Contained | Use |
|---|---|---|
| Pancreatin / Pancrease | Amylase, lipase, protease | Chronic pancreatitis, cystic fibrosis, post-pancreatectomy |
| Lactase (Lactaid) | Lactase (β-galactosidase) | Lactose intolerance |
| Papain | Proteolytic enzyme (from papaya) | Digestive aid, wound debridement |
| Drug | Enzyme Inhibited | Therapeutic Use |
|---|---|---|
| Statins (atorvastatin) | HMG-CoA reductase | ↓ Cholesterol |
| Aspirin | Cyclooxygenase (COX) | Anti-platelet, anti-inflammatory |
| ACE inhibitors (enalapril) | Angiotensin-converting enzyme | Hypertension, heart failure |
| Methotrexate | Dihydrofolate reductase (DHFR) | Cancer, autoimmune disease |
| Allopurinol | Xanthine oxidase | Gout (↓ uric acid) |
| Neostigmine | Acetylcholinesterase | Myasthenia gravis |
| Metformin | Complex I (NADH dehydrogenase) | Type 2 diabetes |
| Penicillin | Transpeptidase | Bacterial cell wall synthesis inhibition |
| Oseltamivir (Tamiflu) | Neuraminidase | Influenza |
| Enzyme | Source | Use |
|---|---|---|
| Collagenase (Santyl) | Clostridium histolyticum | Enzymatic debridement of chronic wounds, burns |
| Papain-urea | Papaya | Wound debridement |
| Hyaluronidase | Testicular extract | Increases tissue permeability; used to facilitate drug diffusion (e.g., local anaesthetic spread) |
| Enzyme | Use |
|---|---|
| L-Asparaginase | Depletes asparagine → kills leukaemia cells (ALL) that cannot synthesize asparagine; used in Acute Lymphoblastic Leukaemia (ALL) treatment |
| Aromatase inhibitors (anastrozole) | Inhibit CYP19 (aromatase) → ↓ estrogen → used in estrogen-receptor positive breast cancer |
| Enzyme | Use |
|---|---|
| DNase (Dornase alfa / Pulmozyme) | Breaks down DNA in thick mucus of cystic fibrosis patients → improves lung function |
| Rasburicase | Converts uric acid to allantoin → treats tumour lysis syndrome |
| Imiglucerase | Gaucher disease (ERT — see above) |
| Factor VIII (a protease cofactor) | Haemophilia A (replacement therapy) |
| Streptokinase | Thrombolysis (see above) |
| Organ/System | Enzyme Marker |
|---|---|
| Heart (MI) | CK-MB, LDH1 |
| Liver (hepatitis) | ALT, AST, GGT, ALP |
| Pancreas | Lipase, Amylase |
| Bone | ALP (bone isoform) |
| Muscle | CK-MM, Aldolase |
| Prostate | PSA |
| Category | Example |
|---|---|
| ERT (Lysosomal storage) | Imiglucerase (Gaucher), Myozyme (Pompe) |
| Thrombolytics | Streptokinase, tPA, Urokinase |
| Digestive | Pancreatin, Lactase |
| Cancer | L-Asparaginase (ALL) |
| Wound care | Collagenase, Hyaluronidase |
| Cystic fibrosis | DNase (Pulmozyme) |
| Enzyme inhibitor drugs | Statins, ACE inhibitors, Aspirin, Allopurinol |
| Source | Pages |
|---|---|
| Lippincott Illustrated Reviews: Biochemistry, 8th ed. | pp. 703–705 (diagnostic enzyme markers, AST/ALT, ALP) |
| Quick Compendium of Clinical Pathology, 5th ed. | pp. 2–4 (CK, LDH, ALP, acid phosphatase, GGT) |
| Thompson & Thompson Genetics & Genomics in Medicine, 9th ed. | pp. 226–228 (ERT — Gaucher, Pompe, lysosomal storage diseases) |
| Emery's Elements of Medical Genetics and Genomics | p. 226 (ERT, ADA-PEG, enzyme/protein replacement) |
| Goodman & Gilman's Pharmacological Basis of Therapeutics | pp. 120–127 (enzyme inhibitors as drugs, CYP450, aromatase) |
| Katzung's Basic and Clinical Pharmacology, 16th ed. | pp. 95–103 (enzyme inhibitor drugs, Phase I reactions) |