The energy conserving methyltetrahydromethanopterin: coenzyme M 
methyltransferase complex from methanogenic archaea: function of the subunit 
MtrH

Hippler, B; Thauer, Rudolf K.

doi:10.1016/S0014-5793(99)00429-9

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The energy conserving methyltetrahydromethanopterin: coenzyme M methyltransferase complex from methanogenic archaea: function of the subunit MtrH

MPS-Authors

Hippler, B
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

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Thauer, Rudolf K.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;

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https://doi.org/10.1016/S0014-5793(99)00429-9
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Citation

Hippler, B., & Thauer, R. K. (1999). The energy conserving methyltetrahydromethanopterin: coenzyme M methyltransferase complex from methanogenic archaea: function of the subunit MtrH. FEBS Letters, 449(2-3), 165-168. doi:10.1016/S0014-5793(99)00429-9.

Cite as: https://hdl.handle.net/21.11116/0000-000F-ADED-4

Abstract

In methanogenic archaea the transfer of the methyl group of
N-5-methyltetrahydromethanopterin to coenzyme M is coupled with energy
conservation. The reaction is catalyzed by a membrane associated
multienzyme complex composed of eight different subunits MtrA-H. The 23
kDa subunit MtrA harbors a corrinoid prosthetic group which is
methylated and demethylated in the catalytic cycle. We report here that
the 34 kDa subunit MtrH catalyzes the methylation reaction, MtrH was
purified and shown to exhibit methyltetrahydromethanopterin
:cob(I)alamin methyltransferase activity. Sequence comparison revealed
similarity of MtrH with MetH from Escherichia coli and AcsE from
Clostridium thermoaceticum: both enzymes exhibit methyltetrahydrofolate:
cob(I)alamin methyltransferase activity. (C) 1999 Federation of European
Biochemical Societies.