This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Masai, E.
Right arrow Articles by Fukuda, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Masai, E.
Right arrow Articles by Fukuda, M.

 Previous Article  |  Next Article 

Journal of Bacteriology, March 2003, p. 1768-1775, Vol. 185, No. 6
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.6.1768-1775.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Roles of the Enantioselective Glutathione S-Transferases in Cleavage of ß-Aryl Ether

Eiji Masai,1* Atsushi Ichimura,1 Yusuke Sato,1 Keisuke Miyauchi,1 Yoshihiro Katayama,2 and Masao Fukuda1

Department of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188,1 Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan2

Received 12 August 2002/ Accepted 11 December 2002

Cleavage of the ß-aryl ether linkage is the most important process in lignin degradation. Here we characterize the three tandemly located glutathione S-transferase (GST) genes, ligF, ligE, and ligG, from low-molecular-weight lignin-degrading Sphingomonas paucimobilis SYK-6, and we describe the actual roles of these genes in the ß-aryl ether cleavage. Based on the identification of the reaction product by electrospray ionization-mass spectrometry, a model compound of ß-aryl ether, {alpha}-(2-methoxyphenoxy)-ß-hydroxypropiovanillone (MPHPV), was transformed by LigF or LigE to guaiacol and {alpha}-glutathionyl-ß-hydroxypropiovanillone (GS-HPV). This result suggested that LigF and LigE catalyze the nucleophilic attack of glutathione on the carbon atom at the ß position of MPHPV. High-pressure liquid chromatography-circular dichroism analysis indicated that LigF and LigE each attacked a different enantiomer of the racemic MPHPV preparation. The ligG gene product specifically catalyzed the elimination of glutathione from GS-HPV generated by the action of LigF. This reaction then produces an achiral compound, ß-hydroxypropiovanillone, which is further degraded by this strain. Disruption of the ligF, ligE, and ligG genes in SYK-6 showed that ligF is essential to the degradation of one of the MPHPV enantiomers, and the alternative activities which metabolize the substrates of LigE and LigG are present in this strain.

* Corresponding author. Mailing address: Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan. Phone: 81-258-47-9428. Fax: 81-258-47-9450. E-mail: emasai{at}vos.nagaokaut.ac.jp.

Journal of Bacteriology, March 2003, p. 1768-1775, Vol. 185, No. 6
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.6.1768-1775.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Sato, Y., Moriuchi, H., Hishiyama, S., Otsuka, Y., Oshima, K., Kasai, D., Nakamura, M., Ohara, S., Katayama, Y., Fukuda, M., Masai, E. (2009). Identification of Three Alcohol Dehydrogenase Genes Involved in the Stereospecific Catabolism of Arylglycerol-{beta}-Aryl Ether by Sphingobium sp. Strain SYK-6. Appl. Environ. Microbiol. 75: 5195-5201 [Abstract] [Full Text]  
  • Huang, Y., Xun, R., Chen, G., Xun, L. (2008). Maintenance Role of a Glutathionyl-Hydroquinone Lyase (PcpF) in Pentachlorophenol Degradation by Sphingobium chlorophenolicum ATCC 39723. J. Bacteriol. 190: 7595-7600 [Abstract] [Full Text]  
  • Kanai, T., Takahashi, K., Inoue, H. (2006). Three Distinct-Type Glutathione S-Transferases from Escherichia coli Important for Defense against Oxidative Stress. J Biochem 140: 703-711 [Abstract] [Full Text]  
  • Tocheva, E. I., Fortin, P. D., Eltis, L. D., Murphy, M. E. P. (2006). Structures of Ternary Complexes of BphK, a Bacterial Glutathione S-Transferase That Reductively Dechlorinates Polychlorinated Biphenyl Metabolites. J. Biol. Chem. 281: 30933-30940 [Abstract] [Full Text]  
  • Jaeger, T., Arsic, M., Mayer, C. (2005). Scission of the Lactyl Ether Bond of N-Acetylmuramic Acid by Escherichia coli "Etherase". J. Biol. Chem. 280: 30100-30106 [Abstract] [Full Text]  
  • Kasai, D., Masai, E., Miyauchi, K., Katayama, Y., Fukuda, M. (2005). Characterization of the Gallate Dioxygenase Gene: Three Distinct Ring Cleavage Dioxygenases Are Involved in Syringate Degradation by Sphingomonas paucimobilis SYK-6. J. Bacteriol. 187: 5067-5074 [Abstract] [Full Text]  
  • Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M., Park, J. T. (2005). Recycling of the Anhydro-N-Acetylmuramic Acid Derived from Cell Wall Murein Involves a Two-Step Conversion to N-Acetylglucosamine-Phosphate. J. Bacteriol. 187: 3643-3649 [Abstract] [Full Text]  
  • Kasai, D., Masai, E., Miyauchi, K., Katayama, Y., Fukuda, M. (2004). Characterization of the 3-O-Methylgallate Dioxygenase Gene and Evidence of Multiple 3-O-Methylgallate Catabolic Pathways in Sphingomonas paucimobilis SYK-6. J. Bacteriol. 186: 4951-4959 [Abstract] [Full Text]  
  • Masai, E., Sasaki, M., Minakawa, Y., Abe, T., Sonoki, T., Miyauchi, K., Katayama, Y., Fukuda, M. (2004). A Novel Tetrahydrofolate-Dependent O-Demethylase Gene Is Essential for Growth of Sphingomonas paucimobilis SYK-6 with Syringate. J. Bacteriol. 186: 2757-2765 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»