Abstract
The regulation of nitrile-hydratase biosynthese was studied in Brevibacterium sp R 312. Enzyme biosynthesis was not influenced by any carbon and nitrogen source used in the growth medium. It was, however, repressed by amide and amide analogues. Acetamide repressed nitrile-hydratase biosynthesis and induced the wide-spectrum amidase. Therefore, it appeared reasonable to hypothesize a single repressor gene for the nitrile-hydratase/wide-spectrum amidase system.
Similar content being viewed by others
References
ArnaudA., GalzyP. & JallageasJ. C. (1976a). Remarques sur l'activité nitrilasique de quelques bactéries. C.R. Acad. Sci. Paris 283: 571–573
ArnaudA., GalzyP. & JallageasJ. C. (1976b) Etude de l'activité nitrilasique de quelques bactéries. Rev. Ferment. Ind. Aliment. 31: 39–44
ArnaudA., GalzyP. & JallageasJ. C. (1976c) Amidase activity of some bacteria. Folia Microbiol. 21: 178–184
ArnaudA., GalzyP. & JallageasJ. C. (1977) Etude de l'acétonitrilase d'une souche de Brevibacterium. Agric. Biol. Chem. 41: 2183–2191
BrammarW. J. & ClarkeP. H. (1964) Induction and repression of Pseudomonas aeruginosa amidase. J. Gen. Microbiol. 37: 307–319
BuiK., ArnaudA. & GalzyP. (1982) A new method to prepare amides by bioconversion of corresponding nitriles. Enzyme Microb. Technol. 4: 195–197
BuiK., FradetH., ArnaudA. & GalzyP. (1984a) A nitrile hydratase with a wide-substrate spectrum produced by a Brevibacterium sp. J. Gen. Microbiol. 130: 89–93
BuiK., FradetH., MaestracciM., ThiéryA., ArnaudA., & GalzyP. (1984b) Utilization of a nitrile hydratase for the production of very pure amides from corresponding nitriles. Fine Chemicals and Pharmaceuticals. Biocatalysts. Third European Congress on Biotechnology 1: 415–423
BuiK., MaestracciM., ThiéryA., ArnaudA. & GalzyP. (1984c) A note on the enzymic action and biosynthesis of a nitrile hydratase from a Brevibacterium sp. J. Appl. Bacteriol. 57: 183–190
BuiK., FradetH., ThiéryA., MaestracciM., ArnaudA. & GalzyP. (1984d) Use of NMR and GLC for the study of microbial nitrile hydratases and amidases. Anal. Chim. Acta 163: 315–322
JallageasJ. C. ArnaudA. & GalzyP. (1978a) Etude de l'acétamidase d'une souche de Brevibacterium sp. J. Gen. Appl. Microbiol. 24: 103–114
JallageasJ. C., ArnaudA. & GalzyP. (1978b) Application de la chromatographie en phase gazeuse à l'étude des nitrilases et amidases. J. Chromatogr. 166: 181–187
JallageasJ. C., ArnaudA. & GalzyP. (1979) Remarques sur le spectre d'activité amidasique d'un mutant de Brevibacterium. C.R. Acad. Sci. Paris 288: 655–658
JallageasJ. C., ArnaudA. & GalzyP. (1980) Bioconversions of nitriles and their applications. Adv. Biochem. Eng. 14: 1–32
MaestracciM., ThiéryA., BuiK., ArnaudA. & GalzyP. (1984) Activity and regulation of an amidase (acylamide amidohydrolase E.C. 3.5.1.4) with a wide substrate spectrum from a Brevibacterium sp. Arch. Microbiol. 138: 315–320
MagasanikB. (1961) Catabolite repression. Cold Spring Harbor Symp. Quant. Biol. 26: 249–256
Thiéry, A., Maestracci, M., Arnaud, A. & Galzy, P. (1986) Nitriles as growth substrates for Brevibacterium sp. R 312 and its mutant M2. Zbl. Mikrobiol. (in press)
TodaK. (1981) Induction and repression of enzymes in microbial culture. J. Chem. Techn. Biotechnol. 31: 775–790
ZimmermannF. K. & ScheelI. (1977) Mutants of Saccharomyces cerevisiae resistant to carbon catabolite repression. Molec. Gen. Genet. 154: 75–82
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Tourneix, D., Thiéry, A., Maestracci, M. et al. Regulation of nitrile-hydratase synthesis in a Brevibacterium species. Antonie van Leeuwenhoek 52, 173–182 (1986). https://doi.org/10.1007/BF00429321
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF00429321