4-Acetamidobutyrate Deacetylase in the Yeast Candida boidinii Grown on Putrescine or Spermidine as Sole Nitrogen Source and Its Probable Role in Polyamine Catabolism

References

1. Andrews P. 1970; Estimation of molecular size and molecular weights of biological compounds by gel filtration. Methods of Biochemical Analysis 18:1–53
   [Google Scholar]
2. Bergmeyer H. U. (editor). 1974; Methods of Enzymatic Analysis, vols 1 and 2, pp. 429:574–613 2nd English edn. Weinheim: Verlag-Chemie.
   [Google Scholar]
3. Brook D. F., Large P. J. 1976; A steady-state kinetic study of the reaction catalysed by the secondary-amine mono-oxygenase of Pseudomonas aminovorans. Biochemical Journal 157:197–205
   [Google Scholar]
4. Chibata I., Tosa T., Ishikawa T. 1964; On the substrate specificity of the bacterial ε-lysine acylase. Archives of Biochemistry and Biophysics 104:231–237
   [Google Scholar]
5. Davis B. J. 1964; Disc electrophoresis II. Method and application to human serum proteins. Annals of the New York Academy of Sciences 121:404–427
   [Google Scholar]
6. Fujimoto D., Koyama T., Tamiya N. 1968; N-acetyl-β-alanine deacetylase in hog kidney. Biochimica et biophysica acta 167:407–413
   [Google Scholar]
7. Gaillardin C., Fournier P., Sylvestre G., Heslot H. 1976; Mutants of Saccharomycopsis lipolytica defective in lysine catabolism. Journal of Bacteriology 125:48–57
   [Google Scholar]
8. Green J., Haywood G. W., Large P. J. 1983; Serological differences between the multiple amine oxidases of yeasts and comparison of the specificities of the purified enzymes from Candida utilis and Pichia pastoris. Biochemical Journal 211:481–493
   [Google Scholar]
9. Greenstein J. P., Winitz M. 1961; Enzymes involved in the determination, characterization and preparation of the amino acids. Chemistry of the Amino Acids volume 2, pp. 1753–1767 New York: John Wiley & Sons.
   [Google Scholar]
10. Guengerich F. P., Broquist H. P. 1976; Lysine catabolism in Rhizoctonia leguminicola and related fungi. Journal of Bacteriology 126:338–347
    [Google Scholar]
11. Haywood G. W., Large P. J. 1981; Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source. Biochemical Journal 199:187–201
    [Google Scholar]
12. Haywood G. W., Large P. J. 1984; Partial purification of a peroxisomal polyamine oxidase from Candida boidinii and its role in growth on spermidine as sole nitrogen source. Journal of General Microbiology 130:1123–1136
    [Google Scholar]
13. Haywood G. W., Large P. J. 1985; The occurrence, subcellular localization and partial purification of diamine acetyltransferase in the yeast Candida boidinii grown on spermidine or putrescine as sole nitrogen source. European Journal of Biochemistry 148:277–283
    [Google Scholar]
14. Inoue A., Fujimoto D. 1969; Enzymatic deacetylation of histone. Biochemical and Biophysical Research Communications 36:146–150
    [Google Scholar]
15. Jakoby W. B. 1962a; Enzymes of γ-aminobutyrate metabolism (bacterial). Methods in Enzymology 5:765–777
    [Google Scholar]
16. Jakoby W. B. 1962b; γ-Aminobutyrate and α-ketoglutarate assay. Methods in Enzymology 5:777–778
    [Google Scholar]
17. Libby P. R. 1970; Activity of histone deacetylase in rat liver and Novikoff hepatoma. Biochimica et biophysica acta 213:234–236
    [Google Scholar]
18. Libby P. R. 1978; Properties of an acetylspermidine deacetylase from rat liver. Archives of Biochemistry and Biophysics 188:360–363
    [Google Scholar]
19. Martin R. G., Ames B. N. 1961; A method for determining the sedimentation behavior of enzymes: application to protein mixtures. Journal of Biological Chemistry 236:1372–1379
    [Google Scholar]
20. Middelhoven W. J., Hoogkamer-Te Niet M. C., Kreger-Van Rij N. J. W. 1984; Trichosporon adeninovorans sp. nov., a yeast species utilizing adenine, xanthine, uric acid, putrescine and primary n-alkylamines as the sole source of carbon, nitrogen and energy. Antonie van Leeuwenhoek 50:369–378
    [Google Scholar]
21. Middelhoven W. J., De Kievit H., Biesbroek A. L. 1985; Yeast species utilizing uric acid, adenine, n-alkylamines and diamines as sole source of carbon and energy. Antonie van Leeuwenhoek (in the Press). Antonie van Leeuwenhoek 50:369–378
    [Google Scholar]
22. Paik W. K., Bloch-Frankenthal L., Birnbaum S. M., Winitz M., Greenstein J. P. 1957; ε-Lysine acylase. Archives of Biochemistry and Biophysics 69:56–66
    [Google Scholar]
23. Pegg A. E., Matsui I., Seely J. E., Pritchard M. L., Pösö H. 1981; Formation of putrescine in rat liver. Medical Biology 59:327–333
    [Google Scholar]
24. Satake K., Okuyama T., Ohashi M., Shinoda T. 1960; The spectrophotometric determination of amine, amino acid and peptide with 2,4,6-trinitrobenzene 1-sulfonic acid. Journal of Biochemistry 47:654–660
    [Google Scholar]
25. Seiler N., Al-Therib M. J. 1974a; Putrescine catabolism in mammalian brain. Biochemical Journal 144:29–35
    [Google Scholar]
26. Seiler N., Al-Therib M. J. 1974b; Acetyl-CoA: l,4-diaminobutane N-acetyltransferase. Occurrence in vertebrate organs and subcellular localization. Biochimica et biophysica acta 354:206–212
    [Google Scholar]
27. Seiler N., Schmidt-Glenewinkel T., Sarhan S. 1979; On the formation of γ-aminobutyric acid from putrescine in brain. Journal of Biochemistry 86:277–278
    [Google Scholar]
28. Seiler N., Bolkenius F. N., Knödgen B., Haegele K. 1980; The determination of N ¹-acetylspermine in mouse liver. Biochimica et bio-physica acta 676:1–7
    [Google Scholar]
29. Shepherd D., Garland P. B. 1969; Citrate synthase from rat liver. Methods in Enzymology 13:11–16
    [Google Scholar]
30. Tabor H., Tabor C. W., De Meis L. 1971; Chemical synthesis of N-acetyl-l,4-diaminobutane, N ¹-acetylspermidine and N ⁸-acetylspermidine. Methods in Enzymology 17B:829–833
    [Google Scholar]
31. Yonaha K., Suzuki K., Minei H., Toyama S. 1983; Distribution of ω-amino acid: pyruvate transaminase and aminobutyrate: α-ketoglutarate transaminase in micro-organisms. Agricultural and Biological Chemistry 47:2257–2265
    [Google Scholar]