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Information on EC 2.1.1.86 - tetrahydromethanopterin S-methyltransferase
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2.1.1.86 tetrahydromethanopterin S-methyltransferaseIUBMB Comments
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 .
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Word Map
- 2.1.1.86
-
methanogen
- methanobacterium
- thermoautotrophicum
-
methanosarcina
-
methanogenesis
- corrinoid
-
energy-conserving
- extorquens
-
methanopyrus
-
corrinoid-containing
- kandleri
- barkeri
-
h2-forming
- mazei
- n5,n10-methylenetetrahydromethanopterin
-
formyltransferase
-
methane-producing
-
cobiamide
-
tiiii
-
mumol.min-1.mg
- methanofuran
-
methylotrophy
-
methenyl
- formylmethanofuran
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
h4mpt, n5-methyltetrahydromethanopterin:coenzyme m methyltransferase, ma4384, mtra-h, mtra-h complex, tetrahydromethanopterin methyltransferase, methyl-tetrahydromethanopterin:coenzyme-m methyltransferase, n5-methyltetrahydromethanopterin coenzyme m methyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-methyl-5,6,7,8-tetrahydromethanopterin:coenzyme M methyltransferase
-
5-methyl-5,6,7,8-tetrahydrosarcinapterin:coenzyme M methyltransferase
-
CH3-H4MPT: CoM-SH methyltransferase complex
H,MPT:coenzyme M methyltransferase
methyl-tetrahydromethanopterin:coenzyme M methyltransferase complex
MTR
MtrA-H complex
N5-methyl-tetrahydromethanopterin: coenzyme M methyltransferase
-
-
N5-methyltetrahydromethanopterin: coenzyme M methyltransferase
N5-methyltetrahydromethanopterin:coenzyme M methyltransferase
H,MPT:coenzyme M methyltransferase
-
H,MPT:coenzyme M methyltransferase
-
methyl-tetrahydromethanopterin:coenzyme M methyltransferase complex
-
-
methyl-tetrahydromethanopterin:coenzyme M methyltransferase complex
-
methyl-tetrahydromethanopterin:coenzyme M methyltransferase complex
-
N5-methyltetrahydromethanopterin: coenzyme M methyltransferase
-
N5-methyltetrahydromethanopterin: coenzyme M methyltransferase
-
N5-methyltetrahydromethanopterin:coenzyme M methyltransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in = 5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
5-methyl-5,6,7,8-tetrahydromethanopterin:coenzyme-M 2-methyltransferase (Na+-transporting)
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].
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CAS REGISTRY NUMBER
COMMENTARY
103406-60-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+
-
-
-
r
5,6,7,8-tetrahydromethanopterin + methylcob(III)alamin
5-methyl-5,6,7,8-tetrahydromethanopterin + cob(III)alamin
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
-
-
-
r
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in
5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
5-methyl-5,6,7,8-tetrahydrosarcinapterin + coenzyme M
5,6,7,8-tetrahydrosarcinapterin + methyl-coenzyme M
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
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
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
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
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
the enzyme uses a transmethylation reaction to drive an energy-conserving sodium ion pump
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
the enzyme uses a transmethylation reaction to drive an energy-conserving sodium ion pump
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
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
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
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
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
-
-
-
r
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
-
involved in the formation of methane from CO
-
r
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in
5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
-
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in
5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
-
-
-
ir
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in
5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in
5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
-
-
?
methylcobalamin + 2-mercaptoethanesulfonate
?
at 13.6% of the activity compared to 5-methyl-5,6,7,8-tetrahydromethanopterin
-
?
methylcobalamin + 2-mercaptoethanesulfonate
?
at 13.6% of the activity compared to 5-methyl-5,6,7,8-tetrahydromethanopterin
-
?
N5-methyltetrahydrofolate + 2-mercaptoethanesulfonate
?
at 31.8% of the activity compared to 5-methyl-5,6,7,8-tetrahydromethanopterin
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+
-
-
-
-
r
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
-
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + H+
5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M
-
-
-
-
r
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in
5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
5-methyl-5,6,7,8-tetrahydrosarcinapterin + coenzyme M
5,6,7,8-tetrahydrosarcinapterin + methyl-coenzyme M
-
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
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
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
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
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate
5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate
-
involved in the formation of methane from CO
-
r
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in
5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
-
-
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in
5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
-
-
-
-
ir
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in
5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
-
-
-
?
5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+/in
5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+/out
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.135
5-Methyl-5,6,7,8-tetrahydromethanopterin
at 37°C in 50 mM MOPS-KOH (pH 7.0)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
-
sharp decrease in activity below pH 6.0 and above pH 7.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O59640: subunit A, P80655: subunit B, O59638: subunit C, P80653: subunit D, P80651: subunit E, P80654: subunit F, P80656: subunit G, P80650: subunit H
SwissProt
brenda
P80655: subunit B, P80653: subunit D, P80651: subunit E, P80654: subunit F, P80656: subunit G, P80650: subunit H
SwissProt
brenda
O59640: subunit A, P80655: subunit B, O59638: subunit C, P80653: subunit D, P80651: subunit E, P80654: subunit F, P80656: subunit G, P80650: subunit H
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
membrane-associated enzyme
brenda
membrane associated enzyme
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
Show AA Sequence and Transmembrane Helices (2586 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
13000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
20000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
28000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
34000
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
380000
non-denaturing gradient PAGE
430000
-
laser induced liquid bead ion desorption mass spectrometry or gel filtration and multi-angle light scattering
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
?
-
x * 34000 + x * 28000 + x * 20000 + x * 13000 + x * 12000 + x * 9000, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with either hydroxocobalamin or methylcobalamin, vapor diffusion method, using 26% (w/v) PEG 3000, 2.2 M DL-malate pH 7.6, 100 mM Tris-HCl pH 8.0
-
in complex with either hydroxocobalamin or methylcobalamin, vapor diffusion method, using 26% (w/v) PEG 3000, 100 mM Na citrate pH 5.5
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTAmtr
-
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE Sepharose column chromatography and Superose-6 gel filtration
-
Ni2+ -charged HiTrap column chromatography
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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
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sauer, F.D.
Tetrahydromethanopterin methyltransferase, a component of the methane synthesizing complex of Methanobacterium thermoautotrophicum
Biochem. Biophys. Res. Commun.
136
542-547
1986
Methanothermobacter thermautotrophicus
brenda
Welander, P.V.; Metcalf, W.W.
Mutagenesis of the C1 oxidation pathway in Methanosarcina barkeri: new insights into the Mtr/Mer bypass pathway
J. Bacteriol.
190
1928-1936
2008
Methanosarcina barkeri
brenda
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 (P80655 and P80653 and P80651 and P80654 and P80656 and P80650), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (P80655 and P80653 and P80651 and P80654 and P80656 and P80650)
brenda
Lienard, T.; Gottschalk, G.
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 (O59640 and P80655 and O59638 and P80653 and P80651 and P80654 and P80656 and P80650), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (O59640 and P80655 and O59638 and P80653 and P80651 and P80654 and P80656 and P80650)
brenda
Peterson, J.R.; Labhsetwar, P.; Ellermeier, J.R.; Kohler, P.R.; Jain, A.; Ha, T.; Metcalf, W.W.; Luthey-Schulten, Z.
Towards a computational model of a methane producing archaeum
Archaea
2014
898453
2014
Methanosarcina acetivorans
brenda
Vepachedu, V.R.; Ferry, J.G.
Role of the fused corrinoid/methyl transfer protein CmtA during CO-dependent growth of Methanosarcina acetivorans
J. Bacteriol.
194
4161-4168
2012
Methanosarcina acetivorans (Q8THX4), Methanosarcina acetivorans
brenda
Upadhyay, V.; Ceh, K.; Tumulka, F.; Abele, R.; Hoffmann, J.; Langer, J.; Shima, S.; Ermler, U.
Molecular characterization of methanogenic N5-methyl-tetrahydromethanopterin coenzyme M methyltransferase
Biochim. Biophys. Acta
1858
2140-2144
2016
Methanothermobacter marburgensis
brenda
Wagner, T.; Ermler, U.; Shima, S.
MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode
Sci. Rep.
6
28226
2016
Methanocaldococcus jannaschii, Methanothermus fervidus (E3GWY7), Methanothermus fervidus, Methanothermus fervidus ATCC 43054 (E3GWY7)
brenda
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EXTERNAL LINKS (specific for EC-Number 2.1.1.86)
Transporter Classification Database (TCDB): 3.C.1.1.1
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