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Oxidation of methionine and 2-hydroxy 4-methylthiobutanoic acid stereoisomers in chicken tissues

Published online by Cambridge University Press:  09 March 2007

Liliane Dupuis ,
C. Linda Saunderson ,
Antoine Puigserver  and
Patrick Brachet
Liliane Dupuis
Affiliation:
Centre de Biochimie et de Biologie Moléculaire du CNRS, BP 71, 13402 Marseille, Cédex 9, France
C. Linda Saunderson
Affiliation:
Centre de Biochimie et de Biologie Moléculaire du CNRS, BP 71, 13402 Marseille, Cédex 9, France
Antoine Puigserver
Affiliation:
Centre de Biochimie et de Biologie Moléculaire du CNRS, BP 71, 13402 Marseille, Cédex 9, France
Patrick Brachet
Affiliation:
Centre de Biochimie et de Biologie Moléculaire du CNRS, BP 71, 13402 Marseille, Cédex 9, France
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Abstract

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Oxidation of dl-2-hydroxy 4-methylthiobutanoic acid (dl-HMB), dl-methionine (dl-MET) and l-methionine (l-MET) in chicken tissue homogenates was compared using 1-14C-labelled tracers. The pattern of oxidation of the substrates was similar at both low (0.7 mm) and high (20 mm) concentrations. The rate of conversion to 2-keto 4-methylthiobutanoic acid (KMB) was highest for dl-MET and lowest for l-MET in kidney, liver and intestinal mucosa. In breast muscle, rates for dl-MET and l-MET were similar at 0.7 mm, but dl-HMB showed the highest rate at 20 mm. Kidney contained the highest specific activity for oxidation of all three substrates. Raising the pH of liver and kidney homogenates from 7.5 to 8.6 increased the oxidation of dl-MET, exclusively. Experiments with inhibitors of D-2-hydroxy acid dehydrogenase (EC 1.1.99.6) and L-2-hydroxy acid oxidase (EC 1.1.3.15) suggested that d- and l-HMB were stereospecifically oxidized by the enzymes. KMB stimulated l-MET oxidation in kidney yet inhibited l-MET oxidation in liver homogenates. The effect of KMB on dl-MET and dl-HMB oxidation also varied between tissues. Amino-oxyacetate inhibited l-MET oxidation completely and dl-MET and dl-HMB oxidation almost completely in both kidney and liver. L-Cycloserine was less potent than amino-oxyacetate and decreased l-MET oxidation more in kidney than in liver. It can be calculated from the results that, at low substrate concentrations, the liver contributes principally to the whole body oxidation of both dl-HMB and dl-MET. At high (greater than physiological) concentrations, dl-HMB would be oxidized principally in skeletal muscle. At all concentrations, l-MET would be converted to KMB mainly in the muscle.

Keywords

2-Hydroxy 4-methylthiobutanoic acidMethionine oxidationChicken
Type
Research Article
Information
British Journal of Nutrition , Volume 62 , Issue 1 , July 1989 , pp. 63 - 75
Copyright
Copyright © The Nutrition Society 1989

References

REFERENCES

Baker, D.H. & Boebel, K.P. (1980). Utilization of the D- and L-isomers of methionine and methionine hydroxy analogue as determined by chick bioassay. Journal of Nutrition 110, 959–964.CrossRefGoogle Scholar
Benevenga, N.J., Radcliffe, B.C. & Egan, A.R. (1983). Tissue metabolism of methionine in sheep. Australian Journal of Biological Science 36, 475–485.CrossRefGoogle ScholarPubMed
Brachet, P., Dupuis, L. & Puigserver, A. (1986). Comparative intestinal absorption and tissue metabolism of methionine and α-hydroxy γ-methylthiobutyric acid by broiler chicks. Proceedings of the 7th European Poultry Conference, vol. 1, pp. 307–311 [Larbier, M., editor]. Tours, France: World's Poultry Science Association.Google Scholar
Brachet, P. & Puigserver, A. (1987). Transport of methionine hydroxy analog across the brush border membrane of rat jejunum. Journal of Nutrition 117, 1241–1246.CrossRefGoogle ScholarPubMed
Cammack, R. (1969). Assay, purification and properties of mammalian D-2-hydroxy acid dehydrogenase. Biochemical Journal 115, 55–64.CrossRefGoogle ScholarPubMed
Cleland, W.W. (1979). Statistical analysis of enzyme kinetic data. Methods in Enzymology 63A, 103–138.CrossRefGoogle Scholar
Connock, M.J. (1973). Intestinal peroxisomes in goldfish (Carassius auratus). Comparative Biochemistry and Physiology 45A, 945–951.CrossRefGoogle Scholar
Cooper, A.J.L. & Meister, A. (1972). Isolation and properties of highly purified glutamine transaminase. Biochemistry 11, 661–671.CrossRefGoogle ScholarPubMed
Cooper, A.J.L. & Meister, A. (1974). Isolation and properties of a new glutamine transaminase from rat kidney. Journal of Biological Chemistry 249, 2554–2561.CrossRefGoogle ScholarPubMed
Cromartie, T.H. & Walsh, C.T. (1975). Rat kidney L- α-hydroxy acid oxidase. Isolation of enzyme with one flavine coenzyme per two subunits. Biochemistry 14, 2588–2596.Google ScholarPubMed
Dibner, J.J. (1983). Utilization of supplemental methionine sources by primary cultures of chick hepatocytes. Journal of Nutrition 113, 2116–2123.CrossRefGoogle ScholarPubMed
Dibner, J.J. & Knight, C.D. (1984). Conversion of 2-hydroxy-4 (methylthio) butanoic acid to L-methionine in the chick: a stereospecific pathway. Journal of Nutrition 114, 1716–1723.CrossRefGoogle Scholar
Dixon, M. & Kleppe, K. (1965a). d-amino acid oxidase. II. Specificity, competitive inhibition and reaction sequence. Biochimica et Biophysica Acta 96, 368–382.CrossRefGoogle Scholar
Dixon, M. & Kleppe, K. (1965b). d-amino acid oxidase. III. Effect of pH. Biochimica et Biophysica Acta 96, 383–389.CrossRefGoogle Scholar
Featherston, W.R. & Horn, G.W. (1974). Studies on the utilization of the α-hydroxy acid of methionine by chicks fed crystalline amino acids (diets). Poultry Science 53, 680–686.CrossRefGoogle Scholar
Gordon, R.S. & Sizer, I.W. (1955). The biological equivalence of methionine hydroxy analogue. Poultry Science 34, 1198.Google Scholar
Gordon, R.S. & Sizer, I.W. (1965). Conversion of methionine hydroxy analogue to methionine in the chick. Poultry Science 44, 673–678.CrossRefGoogle ScholarPubMed
Graser, T.A., Godel, H.G., Albers, S., Földi, P. & Fürst, P. (1985). An ultrarapid and sensitive high-performance liquid chromatographic method for determination of tissue and plasma free amino acids. Analytical Biochemistry 151, 142–152.CrossRefGoogle Scholar
Hartree, E.F. (1972). Determination of protein. A modification of the Lowry method that gives a linear photometric response. Analytical Biochemistry 48, 422–427.CrossRefGoogle ScholarPubMed
Hauschildt, S. & Brand, K. (1980). Effects of branched-chain α-keto acids on enzymes involved in branched-chain α-keto acid metabolism in rat tissues. Journal of Nutrition 110, 1709–1716.CrossRefGoogle ScholarPubMed
Hopper, S. & Segal, H.L. (1962). Purification and properties of liver glutamic-alanine transaminase from normal and corticoid treated rats. Journal of Biological Chemistry 237, 3189–3195.CrossRefGoogle Scholar
Janski, A.M. & Cornell, N.W. (1981). Inhibition by cycloserine of mitochondrial and cytosolic aspartate aminotransferase in isolated rat hepatocytes. Biochemical Journal 194, 1027–1030.CrossRefGoogle ScholarPubMed
Jones, S.M.A. & Yeaman, S.J. (1986). Oxidative decarboxylation of 4-methylthio-2-oxobutyrate by branched-chain 2-oxo acid dehydrogenase complex. Biochemical Journal 237, 621–623.CrossRefGoogle ScholarPubMed
Langer, B.W. (1965). The biochemical conversion of 2-hydroxy-4-methylthiobutyric acid into methionine by the rat in vitro. Biochemical Journal 95, 683–687.CrossRefGoogle Scholar
Lerner, J., Yankelowitz, S. & Taylor, M.W. (1969). The intestinal absorption of methionine in chickens provided with permanent Thiry-Vella fistulas. Experientia 25, 689–691.CrossRefGoogle ScholarPubMed
Masters, C. & Holmes, R. (1977). Peroxisomes: new aspects of cell physiology and biochemistry. Physiological Reviews 57, 816–882.CrossRefGoogle ScholarPubMed
Mitchell, A.D. & Benevenga, N.J. (1978). The role of transamination in methionine oxidation in the rat. Journal of Nutrition 108, 67–78.CrossRefGoogle ScholarPubMed
Muramatsu, T., Yokota, H., Okumura, J. & Tasaki, I. (1984). Biological efficacy of liquid methionine and methionine hydroxy analogue free acids in chicks. Poultry Science 63, 1453–1456.CrossRefGoogle ScholarPubMed
Nakano, M. & Danowski, T.S. (1966). Crystalline mammalian l-amino acid oxidase from rat kidney mitochondria. Journal of Biological Chemistry 241, 2075–2083.CrossRefGoogle ScholarPubMed
Nakano, M., Ushijima, Y., Saga, M., Tsutsumi, Y. & Asami, H. (1968). Aliphatic L-α-hydroxy acid oxidases from rat livers. Purification and properties. Biochimica et Biophysica Acta 167, 9–22.CrossRefGoogle Scholar
Novikoff, P.M. & Novikoff, A.B. (1972). Peroxisomes in absorptive cells of mammalian small intestine. Journal of Cell Biology 53, 532–560.CrossRefGoogle ScholarPubMed
Odessey, R. & Goldberg, A.L. (1979). Leucine degradation in cell-free extracts of skeletal muscle. Biochemical Journal 178, 475–484.CrossRefGoogle ScholarPubMed
Peters, T.J. (1972). Cited by De Duve, C. (1973). Biochemical studies on the occurrence, biogenesis and life history of mammalian peroxisomes. Journal of Histochemistry and Cytochemistry 21, 941–948.Google Scholar
Robinson, J.C., Keay, L., Molinari, R. & Sizer, I.W. (1962). L-α-hydroxy acid oxidases of hog renal cortex. Journal of Biological Chemistry 237, 2001–2010.CrossRefGoogle ScholarPubMed
Saunderson, C.L. (1985). Comparative metabolism of L-methionine, D,L-methionine and D,L-2-hydroxy-4. methylthiobutanoic acid by broiler chicks. British Journal of Nutrition 54, 621–633.CrossRefGoogle Scholar
Saunderson, C.L. (1987). Effect of fasting and of methionine deficiency on L-methionine, D,L-methionine and d,l- 2-hydroxy-4-methylthiobutanoic acid metabolism in broiler chicks. British Journal of Nutrition 57, 429–437.CrossRefGoogle Scholar
Schreiner, C.L. & Jones, E.E. (1987). Metabolism of methionine and methionine hydroxy analogue by porcine kidney fibroblasts. Journal of Nutrition 117, 1541–1549.CrossRefGoogle ScholarPubMed
Scott, P.J., Visentin, L.P. & Allen, J.M. (1969). The enzymatic characteristics of peroxisomes of amphibian and avian liver and kidney. Annals of the New York Academy of Sciences 168, 244–264.CrossRefGoogle ScholarPubMed
Tubbs, P.K. & Greville, G.D. (1961). The oxidation of D-α-hydroxy acids in animal tissues. Biochemical Journal 81, 104–114.CrossRefGoogle ScholarPubMed