Isolation and characterization of an alcohol dehydrogenase gene from the octylphenol polyethoxylate degrader Pseudomonas putida S-5

Bioscience, Biotechnology and Biochemistry

Volumn 70, Issue 8, 2006, Pages 1855-1863

  Tasaki, Yuji ^a   Yoshikawa, Hiromichi ^b   Tamura, Hiroto ^c  

^a NAGAOKA NATIONAL COLLEGE OF TECHNOLOGY   (Japan)

^b FUKUOKA INSTITUTE OF TECHNOLOGY   (Japan)

^c MEIJO UNIVERSITY   (Japan)

Author keywords

Alcohol dehydrogenase; Alkylphenol polyethoxylate; Biodegradation mechanism; Octylphenol polyethoxylate; Pseudomonas putida

Indexed keywords

ALCOHOLS; ALDEHYDES; BIODEGRADATION; DNA; ENZYMES; ESCHERICHIA COLI; GENES; MOLECULAR BIOLOGY;

ALCOHOL DEHYDROGENASE; ALKYLPHENOL POLYETHOXYLATE; BIODEGRADATION MECHANISM; OCTYLPHENOL POLYETHOXYLATE; PSEUDOMONAS PUTIDA;

GENETIC ENGINEERING;

ALCOHOL DEHYDROGENASE; OCTOXINOL;

AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; CHEMISTRY; DNA SEQUENCE; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; METHODOLOGY; MOLECULAR CLONING; MOLECULAR GENETICS; PSEUDOMONAS PUTIDA; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION;

ALCOHOL DEHYDROGENASE; AMINO ACID SEQUENCE; CLONING, MOLECULAR; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; MOLECULAR SEQUENCE DATA; OCTOXYNOL; PSEUDOMONAS PUTIDA; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SEQUENCE ANALYSIS, DNA; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PSEUDOMONAS PUTIDA;

EID: 33747845275     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60009     Document Type: Article

References (34)

1. White, R., Jobling, S., Hoare, S. A., Sumpter, J. P., and Parker, M. G., Environmentally persistent alkylphenolic compounds are estrogenic. Endocrinology, 135, 175-182 (1994).
2. Laws, S. C., Carey, S. A., Ferrell, J. M., Bodman, G. J., and Cooper, R. L., Estrogenic activity of octylphenol, nonylphenol, bisphenol A and methoxychlor in rats. Toxicol. Sci., 54, 154-167 (2000).
3. White, G. F., Bacterial biodegradation of ethoxylated surfactants. Pestic. Sci., 37, 159-166 (1993).
4. Ahel, M., Hršak, D., and Giger, W., Aerobic transformation of short-chain alkylphenol polyethoxylates by mixed bacterial cultures. Arch. Environ. Contam. Toxicol., 26, 540-548 (1994).
5. Kawai, F., Microbial degradation of polyethers. Appl. Microbiol. Biotechnol., 58, 30-38 (2002).
6. Enokibara, S., and Kawai, F., Purification and characterization of an ether bond-cleaving enzyme involved in the metabolism of polyethylene glycol. J. Ferment. Bioeng., 83, 549-554 (1997).
7. Sugimoto, M., Tanabe, M., Hataya, M., Enokibara, S., Duine, J. A., and Kawai, F., The first step in polyethylene glycol degradation by Sphingomonads proceeds via a flavoprotein alcohol dehydrogenase containing flavin adenine dinucleotide. J. Bacteriol., 183, 6694-6698 (2001).
8. Stevens, P. J. G., and Bukovac, M. J., Studies on octylphenoxy surfactants. Part I. Effects of oxyethylene content on properties of potential relevance to foliar absorption. Pestic. Sci., 20, 19-35 (1987).
9. Knoche, M., and Bukovac, M. J., Studies on octylphenoxy surfactants. XI. Effect of NAA diffusion through the isolated tomato fruit cuticular membrane. Pestic. Sci., 38, 211-217 (1993).
10. Nishio, E., Ichiki, Y., Tamura, H., Morita, S., Watanabe, K., and Yoshikawa, H., Isolation of bacterial strains that produce the endocrine disruptor, octylphenol diethoxylates, in paddy fields. Biosci. Biotechnol. Biochem., 66, 1792-1798 (2002).
11. Sato, H., Shibata, A., Wang, Y., Yoshikawa, H., and Tamura, H., Characterization of biodegradation intermediates of non-ionic surfactants by matrix-assisted laser desorption/ionization-mass spectrometry. 1. Bacterial biodegradation of octylphenol polyethoxylate under aerobic conditions. Polym. Degrad. Stab., 74, 69-75 (2001).
12. 18O-labeled water. Biomacromolecules, 4, 46-51 (2003).
13. Obradors, N., and Aguilar, J., Efficient biodegradation of high-molecular-weight polyethylene glycols by pure cultures of Pseudomonas stutzeri. Appl. Environ. Microbiol., 57, 2383-2388 (1991).
14. Malamy, M. H., and Horecker, B. L., Release of alkaline phosphatase from cells of Escherichia coli upon lysozyme spheroplast formation. Biochemistry, 3, 1889-1893 (1964).
15. Cheng, K.-J., Ingram, J. M., and Costerton, J. W., Release of alkaline phosphatase from cells of Pseudomonas aeruginosa by manipulation of cation concentration and of pH. J. Bacteriol., 104, 748-753 (1970).
16. Berlutti, F., Passariello, C., Selan, L., Thaller, M. C., and Rossolini, G. M., The Chryseobacterium meningosepticum PafA enzyme: prototype of a new enzyme family of prokaryotic phosphate-irrepressible alkaline phosphatases? Microbiology, 147, 2831-2839 (2001).
17. Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
18. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. E., Seidman, J. G., Smith, J. A., and Struhl, K., "Current Protocols in Molecular Biology," John Wiley and Sons, New York, pp. 2.4.1-2.4.2 (1994).
19. O'Sullivan, D. J., and Klaenhammer, T. R., Rapid mini-prep isolation of high-quality plasmid DNA from Lactococcus and Lactobacillus spp. Appl. Environ. Microbiol., 59, 2730-2733 (1993).
20. van Beilen, J. B., Eggink, G., Enequist, H., Bos, R., and Witholt, B., DNA sequence determination and functional characterization of the OCT-plasmid-encoded alkJKL genes of Pseudomonas oleovorans. Mol. Microbiol., 6, 3121-3136 (1992).
21. +-independent 4-nitrobenzyl alcohol dehydrogenase from Pseudomonas sp. strain TW3. J. Bacteriol., 182, 3136-3141 (2000).
22. Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucl. Acids Res., 25, 3389-3402 (1997).
23. Falquet, L., Pagni, M., Bucher, P., Hulo, N., Sigrist, C. J. A., Hofmann, K., and Bairoch, A., The PROSITE database, its status in 2002. Nucl. Acids Res., 30, 235-238 (2002).
24. Nakai, K., and Kanehisa, M., Expert system for predicting protein localization sites in gram-negative bacteria. Proteins, 11, 95-110 (1991).
25. Hirokawa, T., Boon-Chieng, S., and Mitaku, S., SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics, 14, 378-379 (1998).
26. Thompson, J. D., Higgins, D. G., and Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res., 22, 4673-4680 (1994).
27. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
28. Reid, M. F., and Fewson, C. A., Molecular characterization of microbial alcohol dehydrogenases. Crit. Rev. Microbiol., 20, 13-56 (1994).
29. Saito, Y., Ishii, Y., Hayashi, H., Imao, Y., Akashi, T., Yoshikawa, K., Noguchi, Y., Soeda, S., Yoshida, M., Niwa, M., Hosoda, J., and Shimomura, K., Cloning of genes coding for L-sorbose and L-sorbosone dehydrogenases from Gluconobacter oxydans and microbial production of 2-keto-L-gulonate, a precursor of L-ascorbic acid, in a recombinant G. oxydans strain. Appl. Environ. Microbiol., 63, 454-460 (1997).
30. Lamark, T., Kaasen, I., Eshoo, M. W., Falkenberg, P., McDougall, J., and Strøm, A. R., DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli. Mol. Microbiol., 5, 1049-1064 (1991).
31. Wierenga, R. K., Terpstra, P., and Hol, W. G. J., Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol., 187, 101-107 (1986).
32. van Beilen, J. B., Panke, S., Lucchini, S., Franchini, A. G., Röthlisberger, M., and Witholt, B., Analysis of Pseudomonas putida alkane-degradation gene clusters and flanking insertion sequences: evolution and regulation of the alk genes. Microbiology, 147, 1621-1630 (2001).
33. Sato, H., Shibata, A., Yoshikawa, H., and Tamura, H., Biodegradation mechanisms of non-ionic surfactants evaluated by MALDI-MS. J. Mass Spectrom. Soc. Jpn. (in Japanese), 51, 415-420 (2003).
34. Kostichka, K., Thomas, S. M., Gibson, K. J., Nagarajan, V., and Cheng, Q., Cloning and characterization of a gene cluster for cyclododecanone oxidation in Rhodococcus ruber SC1. J. Bacteriol., 183, 6478-6486 (2001).