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Journal Article

Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolases

MPS-Authors
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Vorholt,  Julia A.
external;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

Lidstrom,  Mary E.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

External Resource

https://doi.org/10.1128/jb.181.18.5750-5757.1999
(Publisher version)

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Citation

Vorholt, J. A., Chistoserdova, L., Stolyar, S. M., Thauer, R. K., & Lidstrom, M. E. (1999). Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolases. Journal of Bacteriology, 181(18), 5750-5757. doi:10.1128/JB.181.18.5750-5757.1999.


Cite as: https://hdl.handle.net/21.11116/0000-000F-ADEF-2
Abstract
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.