Abstract
Flavobacterium sp. KI72 metabolizes 6-aminohexanoic acid cyclic dimer, a by-product of nylon manufacture1, through two newly evolved enzymes, 6-aminohexanoic acid cyclic dimer hydrolase (EI)2 and 6-aminohexanoic acid linear oligomer hydrolase (EII)3. These enzymes are active towards man-made compounds, the cyclic dimer and linear oligomers of 6-aminohexanoic acid respectively, but not towards any of the natural amide bonds tested2,3. The structural genes of EI (nylA) and EII (nylB) are encoded on pOAD2, one of three plasmids harboured in Flavobacterium sp. KI724,5. This plasmid contains two kinds of repeated sequence (RS-I and RS-II); one of the two RS-II sequences, RS-IIA, contains the nylB gene6, while the other, RS-IIB, contains a homologous nylB′ gene. From comparisons of the nucleotide sequences and gene products of the nylB and nylB′ genes, we now conclude that EII enzyme is newly evolved by gene duplication followed by base substitutions on the same plasmid.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Kinoshita, S., Kageyama, S., Iba, K., Yamada, Y. & Okada, H. Agric. biol. Chem. 39, 1219–1223 (1975).
Kinoshita, S. et al. Eur. J. Biochem. 80, 489–495 (1977).
Kinoshita, S. et al. Eur. J. Biochem. 116, 547–551 (1981).
Negoro, S. et al. J. Bact. 143, 238–245 (1980).
Negoro, S. & Okada, H. Agric. biol. Chem. 46, 745–750 (1982)
Negoro, S., Taniguchi, T., Kanaoka, M., Kimura, H. & Okada, H. J. Bact. 155, 22–31 (1983).
Maxam, A. M. & Gilbert, W. Meth. Enzym. 65, 499–560 (1980).
Bolivar, F. et al. Gene 2, 95–113 (1977).
Backman, K., Ptashne, M. & Gilbert, W. Proc. natn. Acad. Sci. U.S.A. 73, 4174–4178 (1976).
Shine, J. & Dalgarno, L. Proc. natn. Acad. Sci. U.S.A. 71, 1342–1346 (1974).
Gold, L. et al. A. Rev. Microbiol. 35, 365–403 (1981).
Jacobsen, H., Klenow, H. & Overgaard-Hansen, K. Eur. J. Biochem. 45, 623–627 (1974).
Ouchterlony, Ö Acta path. microbiol. 26, 507–515 (1949).
Paterson, A. & Clarke, P. H. J. gen. Microbiol. 114, 75–85 (1979).
Smith, H. O. & Birnstiel, M. L. Nucleic Acids Res. 3, 2387–2398 (1976).
Tu, C. D. & Cohen, S. N. Gene 10, 177–183 (1980).
Laurell, C. B. Analyt. Biochem. 15, 45–52 (1966).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Okada, H., Negoro, S., Kimura, H. et al. Evolutionary adaptation of plasmid-encoded enzymes for degrading nylon oligomers. Nature 306, 203–206 (1983). https://doi.org/10.1038/306203a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/306203a0
- Springer Nature Limited
This article is cited by
-
Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72: identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipate
Applied Microbiology and Biotechnology (2018)
-
Directed evolution studies with combinatorial libraries of T4 lysozyme mutants
Molecular Diversity (1996)
-
The nylon oligomer biodegradation system ofFlavobacterium andPseudomonas
Biodegradation (1994)
-
Evolution from primordial oligomeric repeats to modern coding sequences
Journal of Molecular Evolution (1987)