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.
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
-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.
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