Abstract
A general l-amino acid oxidase (l-amino acid: oxygen oxidoreductase (deaminating), EC 1.4.3.2.) has been characterized in Corynebacterium. The enzyme is soluble (MW 130 000–140 000) and is active with most l-α-amino acids but not with aspartate, threonine, proline and glycine. It is subject to substrate inhibition. This amino acid oxidase is induced along with catalase by growth in the presence of amino acids as a nitrogen source and is repressed when ammonium ions are present in the medium. Its probable physiological function is to allow the utilization of amino acids as a nitrogen source.
This is a preview of subscription content, log in via an institution to check access.
References
Andrews, P.: The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem. J. 96, 595–606 (1965)
Barksdale, L.: Corynebacterium diphteriae and its relatives. Bact. Rev. 34, 378–422 (1970)
Bender, A. E., Krebs, H. A.: The oxidation of various synthetic α-amino acids by mammalian d-amino acid oxidase, l-amino acid oxidase of cobra venom, and the l- and d-amino acid oxidases of Neurospora crassa. Biochem. J. 46, 210–219 (1950)
Burton, K.: The l-amino acid oxidase of Neurospora. Biochem. J. 50, 258–268 (1951)
Chen, S. S., Walgate, J. H., Duerre, J. A.: Oxidative deamination of sulfur amino acids by bacterial and snake venom l-amino acid oxidase. Arch. Biochem. Biophys. 146, 54–63 (1971)
Coudert, M.: Obtention de mutants excréteurs de lysine chez des souches de Corynebacterium assimilant les hydrocarbures. Thèse de Docteur-Ingénieur Université de Paris VI (1973)
Dixon, M., Webbs, E. C.: Enzymes, 2nd edn. London: Longmans Green 1964
Iizuka, H., Komagata, K.: Microbiological studies on petroleum and natural gas. I. Determination of hydrocarbon-utilizing bacteria. J. gen. appl. Microbiol. 10, 207–221 (1964)
Krishnamurti, V. S., Buckley, P. J., Duerre, J. A.: Pigment formation from l-tryptophan by a particulate fraction from an Achromobacter species. Arch. Biochem. Biophys. 130, 636–645 (1969)
Pelmont, J., Rossat, A. M.: Oxydation membranaire de la l-phénylalanine chez Proteus mirabilis. C. R. Acad. Sci. (Paris) (Ser. D) 271, 869–872 (1970)
Robinson, D. S.: Oxidation of selected alkanes and related compounds by a Pseudomonas strain. Antonie v. Leeuwenhoek 30, 303–316 (1964)
Sallach, H. J., Fahien, L. A.: Nitrogen metabolism of amino acids. In: Metabolic pathways, vol. 3, D. M. Greenberg, ed., pp. 1–94. New York: Academic Press 1969
Stumpf, P. K., Green, D. E.: l-Amino acid oxidase of Proteus vulgaris. J. Biochem. 153, 387–399 (1944)
Vandecasteele, J. P., Hermann, M.: Regulation of a catabolic pathway: lysine degradation in Pseudomonas putida. Europ. J. Biochem. 31, 80–85 (1972)
Zeller, E. A., Maritz, A.: A new l-amino acid oxidase. Helv. chim. Acta 27, 1888–1902 (1944)
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Coudert, M., Vandecasteele, JP. Characterization and physiological function of a soluble l-amino acid oxidase in Corynebacterium . Arch. Microbiol. 102, 151–153 (1975). https://doi.org/10.1007/BF00428360
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00428360