151 5 Establishing a peroxisomal β-oxidation computational kinetic model to understand the effects of amino-acid restriction 44. Jiang, L. L., Miyazawa, S. & Hashimoto, T. Purification and Properties of Rat D-3Hydroxyacyl-CoA Dehydratase: D-3-Hydroxyacyl-CoA Dehydratase/D-3-HydroxyacylCoA Dehydrogenase Bifunctional Protein 1 di(2-ethylhexyl)phthalate; bifunctional protein, enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase bi-functional protein; trifunctional protein, enoyl-CoA hydratase/3-hy-droxyacyl-CoA dehydrogenase/3ketoacyl-CoA thiolase trifunctional protein. Downloaded from. J. Biochem vol. 120 http://jb.oxfordjournals.org/ (1996). 45. Houten, S. M. et al. Peroxisomal L-bifunctional enzyme (Ehhadh) is essential for the production of medium-chain dicarboxylic acids. J Lipid Res 53, 1296–1303 (2012). 46. Dieuaide-noubhani, M., Novikov, D., van Veldhoven, P. P. & Mannaerts, G. P. Identification and characterization of the 2-enoyl-CoA hydratases involved in peroxisomal β-oxidation in rat liver. Biochem. J vol. 321 (1997). 47. Jiang, L. L., Kurosawa, T., Sato, M., Suzuki, Y. & Hashimoto, T. Physiological Role of D-3Hydroxyacyl-CoA Dehydratase/ D-3-Hydroxyacyl-CoA Dehydrogenase Bifunctional Protein 1. J. Biochem vol. 121 http://jb.oxfordjournals.org/ (1997). 48. Cleland, W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects 67, 104–137 (1963). 49. Miyazawa, S., Furuta, S., Osumi, T., Hashimoto, T. & Up, N. Properties of Peroxisomal 3-Ketoacyl-CoA Thiolase from Rat Liver 1. vol. 90 (1981). 50. Antonenkov, V. D., Van Veldhoven, P. P., Waelkens, E. & Mannaerts, G. P. Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver. Biochim Biophys Acta 1737, 136–141 (1999). 51. Antonenkov, V. D., Van Veldhoven, P. P., Waelkens, E. & Mannaerts, G. P. Substrate specificities of 3-oxoacyl-CoA thiolase a and sterol carrier protein 2/3-oxoacyl-coa thiolase purified from normal rat liver peroxisomes. Sterol carrier protein 2/3-oxoacylCoA thiolase is involved in the metabolism of 2-methyl-branched fatty acids and bile acid intermediates. Journal of Biological Chemistry 272, 26023–26031 (1997). 52. Jakobs, B. S. & Wanders, R. J. A. Fatty acid β-oxidation in peroxisomes and mitochondria: The first, unequivocal evidence for the involvement of carnitine in shuttling propionyl-CoA from peroxisomes to mitochondria. Biochem Biophys Res Commun 213, 1035–1041 (1995). 53. Miyazawa, S., Ozasa, H., Osumi, T. & Hashimoto, T. Purification and Properties of Camitine Octanoyltransferase and Camitine Palmitoyltransf erase from Rat Liver 1. J. Biochem 94, 529–542 (1983). 54. Miyazawa, S., Ozasa, H., Furuta, S., Osumi, T. & Hashimoto, T. Purification and Properties of Carnitine Acetyltransferase from Rat Liver. J. Biochem 93, 439–451 (1983). 55. Farrell, S. O., Fiol, C. J., Reddy, J. K. & Bieber, L. L. Properties of purified carnitine acyltransferases of mouse liver peroxisomes. Journal of Biological Chemistry 259, 13089–13095 (1984). 56. Liebermeister, W. & Klipp, E. Bringing metabolic networks to life: Convenience rate law and thermodynamic constraints. Theor Biol Med Model 3, (2006). 57. Hartl, F.-U., Just,’, W. W., Kijster, A. & Schimassek, H. Improved Isolation and Purification of Rat Liver Peroxisomes by Combined Rate Zonal and Equilibrium Density Centrifugation. Arch Biochem Biophys 237, 124–134 (1985).
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