SN1
SHORT NOTE
5M
★ High-yield
Define transamination. Describe its mechanism, significance and clinical applications.
Definition
Transamination = the reversible transfer of an α-amino group from an amino acid to an α-keto acid, forming a new amino acid and a new keto acid.
Amino acid1 + Keto acid2 ↔ Keto acid1 + Amino acid2
Features
- Enzyme — aminotransferase (transaminase)
- Coenzyme — pyridoxal phosphate (vitamin B6) for every transaminase
- Freely reversible; ΔG is near zero
- No free ammonia is released and no nitrogen is lost — it is a redistribution, not an excretion
- α-Ketoglutarate is the usual acceptor, so nitrogen is funnelled into glutamate
- Occurs in cytosol and mitochondria of most tissues, especially liver and muscle
Amino Acids That Do Not Transaminate
- Lysine, threonine, proline and hydroxyproline
- All others do, including the essential ones — which is why their keto acid analogues can substitute for them in the diet
Mechanism — Ping Pong Bi Bi
PLP + amino acid → Schiff base (aldimine) → Tautomerisation → ketimine → Hydrolysis → Keto acid1 released; enzyme now carries pyridoxamine phosphate → Second keto acid binds → Reverse sequence → Amino acid2 released; PLP regenerated
Clinically Important Transaminases
| Enzyme | Reaction | Normal | Raised in |
|---|---|---|---|
| ALT (SGPT) | Alanine + α-KG ↔ pyruvate + glutamate | 7–40 U/L | Liver disease — more specific; very high in viral hepatitis |
| Ast (SGOT) | Aspartate + α-KG ↔ oxaloacetate + glutamate | 10–40 U/L | Liver, myocardial infarction, muscle disease, haemolysis |
CLINICAL PEARL
Ast : ALT ratio — above 2 suggests alcoholic liver disease (ast is also released from mitochondria and ALT synthesis needs B6, which alcoholics lack); below 1 suggests viral hepatitis or fatty liver.
Significance and Applied Aspects
- Collects nitrogen from all amino acids into glutamate, the single substrate for oxidative deamination — the funnel principle
- Allows synthesis of non-essential amino acids from available keto acids
- Links amino acid metabolism to the TCA cycle through pyruvate, oxaloacetate and α-ketoglutarate
- Diagnostic — the transaminases are among the most widely used enzymes in clinical medicine
- Vitamin B6 deficiency impairs all transaminations; a transaminase assay with and without added PLP is used to assess B6 status
All questions in Amino Acid & Protein Metabolism
- Q1Describe the urea cycle with its reactions, site and energetics. Explain its regulation and add a note on the urea cycle disorders. ★
- Q2Describe transamination and deamination. Explain the sources, transport and disposal of ammonia in the body. ★
- Q3Describe the metabolism of phenylalanine and tyrosine. Discuss the disorders arising from blocks in this pathway. ★
- Q4Describe the metabolism of methionine and cysteine. Explain transmethylation, the role of SAM, and the methyl trap hypothesis. ★
- Q5Define nitrogen balance. Describe protein turnover and protein quality. Compare kwashiorkor with marasmus. ★
- SN1Define transamination. Describe its mechanism, significance and clinical applications. ★
- SN2Define hyperammonaemia. Describe its causes, the basis of ammonia toxicity, and its management. ★
- SN3Write a short note on phenylketonuria. ★
- SN4Describe alkaptonuria and albinism with their biochemical basis. ★
- SN5Describe the structure, synthesis and functions of glutathione. ★
- SN6Write a short note on homocystinuria. Differentiate it from Marfan syndrome. ★
- SN7Describe the synthesis and significance of creatine and creatinine. ★