JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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 Sugimoto, M.
Right arrow Articles by Kawai, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sugimoto, M.
Right arrow Articles by Kawai, F.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2001, p. 6694-6698, Vol. 183, No. 22
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.22.6694-6698.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

The First Step in Polyethylene Glycol Degradation by Sphingomonads Proceeds via a Flavoprotein Alcohol Dehydrogenase Containing Flavin Adenine Dinucleotide

Manabu Sugimoto,1 Miwa Tanabe,1 Misako Hataya,1 Shogo Enokibara,2 Johannis A. Duine,1 and Fusako Kawai1,*

Research Institute for Bioresources, Okayama University, Kurashiki, Okayama 710-0046,1 and General Education Course, Kobe University of Commerce, Kobe 651-2197,2 Japan

Received 16 April 2001/Accepted 24 August 2001

Several Sphingomonas spp. utilize polyethylene glycols (PEGs) as a sole carbon and energy source, oxidative PEG degradation being initiated by a dye-linked dehydrogenase (PEG-DH) that oxidizes the terminal alcohol groups of the polymer chain. Purification and characterization of PEG-DH from Sphingomonas terrae revealed that the enzyme is membrane bound. The gene encoding this enzyme (pegA) was cloned, sequenced, and expressed in Escherichia coli. The purified recombinant enzyme was vulnerable to aggregation and inactivation, but this could be prevented by addition of detergent. It is as a homodimeric protein with a subunit molecular mass of 58.8 kDa, each subunit containing 1 noncovalently bound flavin adenine dinucleotide but not Fe or Zn. PEG-DH recognizes a broad variety of primary aliphatic and aromatic alcohols as substrates. Comparison with known sequences revealed that PEG-DH belongs to the group of glucose-methanol-choline (GMC) flavoprotein oxidoreductases and that it is a novel type of flavoprotein alcohol dehydrogenase related (percent identical amino acids) to other, so far uncharacterized bacterial, membrane-bound, dye-linked dehydrogenases: alcohol dehydrogenase from Pseudomonas oleovorans (46%); choline dehydrogenase from E. coli (40%); L-sorbose dehydrogenase from Gluconobacter oxydans (38%); and 4-nitrobenzyl alcohol dehydrogenase from a Pseudomonas species (35%).

* Corresponding author. Mailing address: Research Institute for Bioresources, Okayama University, Kurashiki, Okayama 710-0046, Japan. Phone: 81 86 434 1225. Fax: 81 86 434 1225. E-mail: fkawai{at}rib.okayama-u.ac.jp.

Journal of Bacteriology, November 2001, p. 6694-6698, Vol. 183, No. 22
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.22.6694-6698.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2001 by the American Society for Microbiology. All rights reserved.