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Define coenzymes. Enumerate the coenzymes derived from vitamins with their functions.

Biochemistry · 1st Professional — Pre-Clinical

Definition

Coenzymes = small, heat-stable, non-protein organic molecules that are essential for the activity of certain enzymes, acting as carriers of atoms, groups or electrons.

  • Most coenzymes are derived from water-soluble B-complex vitamins — the reason these vitamins are required in the diet
  • They are loosely bound; a tightly (covalently) bound cofactor is a prosthetic group
  • Coenzymes are regenerated, so they act catalytically and are needed only in small amounts

Coenzymes Derived from Vitamins

VitaminCoenzymeFunctionDeficiency
B1 ThiamineThiamine pyrophosphate (TPP)Oxidative decarboxylation; transketolaseBeri-beri, Wernicke encephalopathy
B2 RiboflavinFMN, FADHydrogen transfer (2H)Angular stomatitis, glossitis
B3 NiacinNAD+, NADP+Hydrogen transfer (2 electrons + H+)Pellagra
B5 PantothenateCoenzyme AAcyl group transferBurning feet syndrome
B6 PyridoxinePyridoxal phosphate (PLP)Transamination, decarboxylation, ala synthasePeripheral neuropathy, sideroblastic anaemia, convulsions
B7 BiotinBiocytinCO2 fixation (carboxylation)Dermatitis; caused by raw egg white (avidin)
B9 FolateTetrahydrofolateOne-carbon transferMegaloblastic anaemia, neural tube defect
B12 CobalaminMethylcobalamin, deoxyadenosylcobalaminMethyl transfer; methylmalonyl-CoA mutaseMegaloblastic anaemia, subacute combined degeneration

Non-vitamin Coenzymes

  • ATP — phosphate and energy transfer
  • S-adenosylmethionine (SAM) — the chief methyl donor
  • UDP-glucose — glycosyl transfer
  • Lipoic acid — acyl transfer in the PDH complex
  • Coenzyme Q — electron transfer in the respiratory chain

Applied Aspects

  • Isoniazid antagonises pyridoxine → peripheral neuropathy; hence pyridoxine is given prophylactically with antitubercular treatment
  • Methotrexate blocks dihydrofolate reductase → folate coenzymes cannot be regenerated; rescued with folinic acid
  • Thiamine must be given before glucose in a malnourished or alcoholic patient — a glucose load without thiamine can precipitate Wernicke encephalopathy
  • Multiple carboxylase deficiency responds to large doses of biotin

All questions in Enzymes

  1. Q1Define enzymes. Classify them according to the IUBMB system and describe the mechanism of enzyme action. Add a note on enzyme specificity. ★
  2. Q2Describe the effect of substrate concentration on enzyme activity. Explain the Michaelis–Menten equation, the significance of Km and the Lineweaver–Burk plot. ★
  3. Q3Classify enzyme inhibition. Describe competitive, non-competitive and uncompetitive inhibition with their effects on Km and Vmax, and give examples. ★
  4. Q4Describe the mechanisms regulating enzyme activity. Explain allosteric regulation, covalent modification and enzyme induction with examples. ★
  5. Q5Describe the diagnostic importance of serum enzymes. Give the enzyme profile in myocardial infarction and liver disease. Add a note on isoenzymes. ★
  6. SN1Define coenzymes. Enumerate the coenzymes derived from vitamins with their functions. ★
  7. SN2Define isoenzymes. Describe the isoenzymes of lactate dehydrogenase and creatine kinase with their clinical significance. ★
  8. SN3Describe allosteric enzymes with their characteristics and examples. Add a note on feedback inhibition. ★
  9. SN4Define zymogens. Give examples and explain their physiological importance. ★
  10. SN5Define Km. Describe its significance with the example of hexokinase and glucokinase. ★
  11. SN6Describe competitive inhibition with its characteristics and medically important examples. ★
  12. SN7Describe the types of enzyme specificity with examples.

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