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Methionine transamination—metabolic function and subcellular compartmentation

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Abstract

Enzymatic activities catalysing the inter-conversion of L-methionine and its oxy analogue 4-methylthio-2-oxobutyric acid (2,4-KMB) were detected in the liver, skeletal muscle and heart of the laboratory rat and of sheep. In both species the highest activity of methionine transamination was found in the liver and was located in the cytoplasm and mitochondria. We propose that physiological and nutritional role of the cytoplasmic methionine transamination is amination of 2,4 KMB and formation of L-methionine while in mitochondria the activity is responsible for disposal of excess methionine is oxidised through oxidative decarboxylation of 2,4 KMB.

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References

  1. Stipanuk MH: Metabolism of sulfur containing amino acids. Ann Rev Nutr 6: 179–209, 1986

    Google Scholar 

  2. Case GL, Benevenga NJ: Evidence for S-adenosylmethionine independent catabolism of methionine in the rat. J Nutr 106: 1721–1736, 1976

    Google Scholar 

  3. Benevenga NJ: Evidence for alternative pathways of methionine catabolism. Adv Nutr Res 6: 1–18, 1984

    Google Scholar 

  4. Blom HJ, Boers GHJ, van den Elzen PAM, Gahl WA, Tangerman A: Transamination of methionine in humans. Clin Sci 76: 43–49, 1989

    Google Scholar 

  5. Mitchell AD, Benevenga NJ: The role of transamination in methionine oxidation in the rat. J Nutr 108: 67–78, 1978

    Google Scholar 

  6. Blom HJ, Boers GHJ, Tangerman A, Gahl WA, Trijbels JMF: Alternative methionine degradation via transamination pathway: an option for therapy for homcytinuria due to cystathionine synthase deficiency. J Inher Metab Dis 14: 375–378, 1991

    Google Scholar 

  7. Benevenga NJ, Egan AR: Quantitative aspects of methionine metabolism. Sulfur amino acids: Biochemical and clinical aspects. Progress in Clin Biol Res 125: 327–341, 1983

    Google Scholar 

  8. Benevenga NJ, Steele RD: Adverse effects of excessive consumption of amino acids. Ann Rev Nutr 4: 157–181, 1984

    Google Scholar 

  9. Cooper AJL, Meister A: Isolation and properties of highly purified glutamine transaminase. Biochemistry 11: 661–671, 1972

    Google Scholar 

  10. Cooper AJL, Meister A: Isolation and properties of a new glutamine transaminase from rat kidney. J Biol Chem 249: 2554–2561, 1974

    Google Scholar 

  11. Cooper AJL: Asparagine transaminas from rat liver. J Biol Chem 252: 2032–2038, 1977

    Google Scholar 

  12. Ikeda T, Konishi Y, Ichichara A: Transaminase of branched chain amino acids. Biochim Biophys Acta 445: 622–631, 1976

    Google Scholar 

  13. Jenkins WT: Special aspect of various transaminases. In: P Christen, DE Metzler (eds) Transaminases. J Wiley & Sons, New York, 1985, pp 365–373

    Google Scholar 

  14. Johnson D, Lardy H: Isolation of liver or kidney mitochondria. In: RW Estabrook, ME Pullman (eds) Methods in Enzymol. Acad Press N.Y., London vol. X 1967, pp 92–101

    Google Scholar 

  15. Lund P: In: HU Bergmeyer, J Bergmeyer, M Grabl (eds) Methods of Enzymatic Analysis. VCH Veinheim vol. VIII, 1985, pp 357–363

    Google Scholar 

  16. Williamson DH: In: HU Bergmeyer, J Bergmeyer, M Grabl (eds) Methods of Enzymatic Analysis. VCH Veinheim vol. VIII, 1985, pp 341–345

    Google Scholar 

  17. Cooper AJL, Meister A: Glutamine transaminase L from rat liver. Meth in Enzymol 113: 338, 1985

    Google Scholar 

  18. Cooper AJL, Meister A: Glutamine transaminase K from rat kidney. Methods in Enzymol 113: 344–349, 1985

    Google Scholar 

  19. Srere PA: Citrate synthase. In: JM Lowenstein (ed.) Methods in Enzymology. Ac Press, New York vol. 13, 1969, pp 3–5

    Google Scholar 

  20. Scisloski PWD, Zolnierowicz S, Zelewski L: Subcellular distribution of isocitrate dehydrogenase in early and term human placenta. Biochem J 214: 339–343, 1983

    Google Scholar 

  21. Gornall AG, Bardawill CJ, David MM: Determination of serum proteins by means of the biuret reaction. J Biol Chem 177: 751–756, 1949

    Google Scholar 

  22. Scislowski PWD, Hokland BM, Davis van Thienen WIA, Bremer J, Davis EJ: Methionine metabolism by rat muscle and other tissues. Biochem J 247: 35–40, 1987

    Google Scholar 

  23. Schmidt E, Schmidt FW: Aminotransferases in human pathology and clinical chemistry. In: P Chriten DE Metzler (eds) Transaminases. J Wiley & Sons, New York, 1985, pp 365–373

    Google Scholar 

  24. Dupuis L, Brachet P, Puigseruer A: Oxidation of a supplemental methionine source L-2-hydroxy-4-methylthiobutanoic acid by pure L-2-hydroxy acid oxidase from chicken liver. J Nutr 120: 1171–1178, 1990

    Google Scholar 

  25. Printen KJ, Brummel MC, Cho ES, Stegink LD: Utilization of D-methionine during total pareneral nutrition in postsurgical patients. Am J Clin Nutr 32: 1200–1205, 1979

    Google Scholar 

  26. Funk MA, Hortin AE, Baker DH: Utilization of D-methionine by growing rats. Nutr Res 10: 1029–1034, 1990

    Google Scholar 

  27. Backlund PS Jr, Smith PA: Methionine synthesis from 5′-methylthioadenosine in rat liver. J Biol Chem 256: 1533–1535, 1981

    Google Scholar 

  28. Cooper AJL, Meister A: Comparative studies of glutamine transaminases from rat tissues. Comp Biochem Physiol 69B: 137–145, 1981

    Google Scholar 

  29. Deuel TF, Louie M, Lerner A: Glutamine synthetase from rat liver. J Biol Chem 253: 6111–6118, 1978

    Google Scholar 

  30. Hutson SM, Rannels S: Characterisation of a mitochondrial transport system for branched chain a-keto acids. J Biol Chem 260: 14189–14193, 1985

    Google Scholar 

  31. Hutson S: pH Regulation of mitochondrial branched chain a-keto acid transport and oxidation in rat heart mitochondria. J Biol Chem 262: 9629–9635, 1987

    Google Scholar 

  32. Soboll S, Lenzen C, Retich D, Grundel S, Ziegler B: Characterisation of glutamine uptake in rat liver mitochondria. Eur J Biochem 197: 113–117, 1991

    Google Scholar 

  33. Jones SMA, Yeaman SJ: Oxidative decarboxylation of 4-methylthio-2-oxo-butyric acid by branched chain 2-oxo acid dehydrogenase complex. Biochem J 237: 621–623, 1986

    Google Scholar 

  34. Cybulski RL, Fisher RR: Mitochondrial neutral amino acid transport: evidence for a carrier mediated mechanism. Biochem 16: 5116–5120, 1977

    Google Scholar 

  35. Lau S, Brantley RK, Thorpe C: 4-thia-trans-2-alkenoyl-CoA derivatives: properties and enzymatic reactions. Biochem 28: 8255–8262, 1989

    Google Scholar 

  36. Harper AE, Miller RH, Block KP: Branched-chain amino acid metabolism. Ann Rev Nutr 4: 409–454, 1984

    Google Scholar 

  37. Block KP, Soemitro S, Heywood BW, Harper AE: Activation of liver branched-chainα-keto acid dehydrogenase in rats by excesses of dietary amino acids. J Nutr 115: 1550–1561, 1985

    Google Scholar 

  38. Wamberg S, Engel K, Kildeberg P: Methionine induced acidosis in the weanling rats. Acta Physiol Scand 129: 575–583, 1987

    Google Scholar 

  39. Merino GE, Jetzer Th, Doizaki WMD, Najarian JS: Methionine induced hepatic coma in dogs. Am J Surg 130: 41–46, 1975

    Google Scholar 

  40. Doyle PT, Adams NR: Toxic effects of large amounts of DL-methionine infused into the rumen of sheep. Austr Vet J 56: 331–334, 1980

    Google Scholar 

  41. Benevenga NJ, Harper AE: Alleviation of methionine and homocystine toxicity in the rat. J Nutr 93: 44–52, 1967

    Google Scholar 

  42. McCully KS: Homocystinuria, arteriosclerosis, methylmalonic aciduria and methyltransferase deficiency: a key case revisited. Nutr Rev 50: 7–12, 1992

    Google Scholar 

  43. Regina M, Korhonen VP, Smith TK, Alakuijala L, Eloranta ThO: Methionine toxicity in the rat in relation to hepatic accumulation of S-adenosylmethionine prevention by dietary stimulation of the hepatic transsulphuration pathway. Arch Biochem Biophys 300: 598–607, 1993

    Google Scholar 

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  1. Rowtt Research Institute, Greenburn Rd., Bucksburn, AB2 9SB, Aberdeen, Scotland

    Piotr W. D. Scislowski & Karen Pickard

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  1. Piotr W. D. Scislowski
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  2. Karen Pickard
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Scislowski, P.W.D., Pickard, K. Methionine transamination—metabolic function and subcellular compartmentation. Mol Cell Biochem 129, 39–45 (1993). https://doi.org/10.1007/BF00926574

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  • DOI: https://doi.org/10.1007/BF00926574

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