Involved in the formation of methane from CO2 in methanogenic archaea. The reaction involves the export of one or two sodium ions. The enzyme from the archaeon Methanobacterium thermoautotrophicum is a membrane-associated multienzyme complex composed of eight different subunits, and contains a 5'-hydroxybenzimidazolyl-cobamide prosthetic group, to which the methyl group is attached during the transfer. A soluble enzyme that is induced by the presence of CO has been reported as well .
5-methyl-5,6,7,8-tetrahydromethanopterin:coenzyme M methyltransferase, 5-methyl-5,6,7,8-tetrahydrosarcinapterin:coenzyme M methyltransferase, CH3-THMPT:HS-CoM methyltransferase, CH3-THMPT:HSCoM methyltransferase, CmtA, cytoplasmic methyltransferase A, H,MPT:coenzyme M methyltransferase, H4MPT, MA4384, methyl-tetrahydromethanopterin methyltransferase, more
Involved in the formation of methane from CO2 in methanogenic archaea. The reaction involves the export of one or two sodium ions. The enzyme from the archaeon Methanobacterium thermoautotrophicum is a membrane-associated multienzyme complex composed of eight different subunits, and contains a 5'-hydroxybenzimidazolyl-cobamide prosthetic group, to which the methyl group is attached during the transfer. A soluble enzyme that is induced by the presence of CO has been reported as well [6].
2-mercaptoethanesulfonate i.e. coenzyme M. The enzyme uses the methylation of coenzyme M (HS-CoM) by methyl-tetrahydromethanopterin to drive an energy-conserving sodium ion pump
2-mercaptoethanesulfonate i.e. coenzyme M. The enzyme uses the methylation of coenzyme M (HS-CoM) by methyl-tetrahydromethanopterin to drive an energy-conserving sodium ion pump. 1.7 mol Na+ per mol of methyl groups transferred are translocated
2-mercaptoethanesulfonate i.e. coenzyme M. The enzyme uses the methylation of coenzyme M (HS-CoM) by methyl-tetrahydromethanopterin to drive an energy-conserving sodium ion pump
2-mercaptoethanesulfonate i.e. coenzyme M. The enzyme uses the methylation of coenzyme M (HS-CoM) by methyl-tetrahydromethanopterin to drive an energy-conserving sodium ion pump. 1.7 mol Na+ per mol of methyl groups transferred are translocated
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
2-mercaptoethanesulfonate i.e. coenzyme M. The enzyme uses the methylation of coenzyme M (HS-CoM) by methyl-tetrahydromethanopterin to drive an energy-conserving sodium ion pump
P80655 and P80653 and P80651 and P80654 and P80656 and P80650
2-mercaptoethanesulfonate i.e. coenzyme M. The enzyme uses the methylation of coenzyme M (HS-CoM) by methyl-tetrahydromethanopterin to drive an energy-conserving sodium ion pump
CmtA is a soluble 5-methyl-5,6,7,8-tetrahydrosarcinapterin:coenzyme M methyltransferase postulated to supplement the membrane-bound 5-methyl-5,6,7,8-tetrahydromethanopterin:coenzyme M methyltransferase during CO-dependent growth of Methanosarcina acetivorans
mutants lacking H4MPT:coenzyme M methyltransferase-encoding operon (DELTAmtr), the methylene-H4MPT reductase encoding gene (DELTAmer), the methylene-H4MPT dehydrogenase-encoding gene (DELTAmtd), and the formyl-methanofuran: H4MPT formyl-transferase-encoding gene (DELTAftr) fail to grow using either methanol or H2/CO2 as a growth substrate, indicating that there is an absolute requirement for the C1 oxidation/reduction pathway for hydrogenotrophic and methylotrophic methanogenesis. Mutants also fail to grow on acetate. DELTAmtr and DELTAmer mutants are capable of producing methane from methanol. Thus, there is an Mtr/Mer bypass pathway that allows oxidation of methanol to the level of methylene-H4MPT in Methanosarcina barkeri. Formaldehyde may be an intermediate in this bypass. DELTAmer and DELTAmtr mutants are able to grow on a combination of methanol plus acetate
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
all of these subunits are shown to be heterologously expressed in minicells of the Escherichia coli mutant DK6. Sequence comparisons with the methyltransferases of thermophilic and hypothermophilic methanogenic archaea
Lienard, T.; Becher, B.; Marschall, M.; Bowien, S.; Gottschalk, G.
Sodium ion translocation by N5-methyltetrahydromethanopterin: coenzyme M methyltransferase from Methanosarcina mazei Gö1 reconstituted in ether lipid liposomes
Eur. J. Biochem.
239
857-864
1996
Methanosarcina mazei, Methanosarcina mazei (P80655 and P80653 and P80651 and P80654 and P80656 and P80650), Methanosarcina mazei DSM 3647 (P80655 and P80653 and P80651 and P80654 and P80656 and P80650)
Cloning, sequencing and expression of the genes encoding the sodium translocating N5-methyltetrahydromethanopterin: coenzyme M methyltransferase of the methylotrophic archaeon Methanosarcina mazei Gö1
FEBS Lett.
425
204-208
1998
Methanosarcina mazei, Methanosarcina mazei (O59640 and P80655 and O59638 and P80653 and P80651 and P80654 and P80656 and P80650), Methanosarcina mazei DSM 3647 (O59640 and P80655 and O59638 and P80653 and P80651 and P80654 and P80656 and P80650)
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2.1.1.86 tetrahydromethanopterin S-methyltransferase
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