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 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 Vorholt, J. A.
Right arrow Articles by Lidstrom, M. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vorholt, J. A.
Right arrow Articles by Lidstrom, M. E.

Journal of Bacteriology, September 1999, p. 5750-5757, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Distribution of Tetrahydromethanopterin-Dependent Enzymes in Methylotrophic Bacteria and Phylogeny of Methenyl Tetrahydromethanopterin Cyclohydrolases

Julia A. Vorholt,1,2 Ludmila Chistoserdova,1 Sergei M. Stolyar,1 Rudolf K. Thauer,2 and Mary E. Lidstrom1,*

Department of Chemical Engineering, University of Washington, Seattle, Washington 98195,1 and Max-Planck-Institut für terrestrische Mikrobiologie and Laboratorium für Mikrobiologie des Fachbereichs Biologie der Philipps-Universität, 35043 Marburg, Germany2

Received 24 March 1999/Accepted 7 July 1999

The methylotrophic proteobacterium Methylobacterium extorquens AM1 possesses tetrahydromethanopterin (H4MPT)-dependent enzymes, which are otherwise specific to methanogenic and sulfate-reducing archaea and which have been suggested to be involved in formaldehyde oxidation to CO2 in M. extorquens AM1. The distribution of H4MPT-dependent enzyme activities in cell extracts of methylotrophic bacteria from 13 different genera are reported. H4MPT-dependent activities were detected in all of the methylotrophic and methanotrophic proteobacteria tested that assimilate formaldehyde by the serine or ribulose monophosphate pathway. H4MPT-dependent activities were also found in autotrophic Xanthobacter strains. However, no H4MPT-dependent enzyme activities could be detected in other autotrophic alpha -proteobacteria or in gram-positive methylotrophic bacteria. Genes encoding methenyl H4MPT cyclohydrolase (mch genes) were cloned and sequenced from several proteobacteria. Bacterial and archaeal Mch sequences have roughly 35% amino acid identity and form distinct groups in phylogenetic analysis.


* Corresponding author. Mailing address: Department of Chemical Engineering, University of Washington, Seattle, WA 98195. Phone: (206) 616-5282. Fax: (206) 616-5721. E-mail: lidstrom{at}u.washington.edu.


Journal of Bacteriology, September 1999, p. 5750-5757, Vol. 181, No. 18
0021-9193/99/$04.00+0
Copyright © 1999, 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 © 1999 by the American Society for Microbiology. All rights reserved.