50187
Ammonium 2-(methylthio)ethanesulfonate
≥97.0% (TLC)
Synonym(s):
Methyl coenzyme M ammonium salt
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About This Item
Empirical Formula (Hill Notation):
C3H11NO3S2
CAS Number:
Molecular Weight:
173.25
MDL number:
UNSPSC Code:
12352106
PubChem Substance ID:
NACRES:
NA.25
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Quality Level
Assay
≥97.0% (TLC)
SMILES string
N.CSCCS(O)(=O)=O
InChI
1S/C3H8O3S2.H3N/c1-7-2-3-8(4,5)6;/h2-3H2,1H3,(H,4,5,6);1H3
InChI key
FSGSBLDVKBYXIK-UHFFFAOYSA-N
Application
Ammonium 2-(methylthio)ethanesulfonate (Methyl coenzyme M) is converted into methane by the enzyme Methyl-coenzyme M reductase (MCR) derived from methanogenic archaea. Methy-coenzyme M is used in studies on methanogenic (methane-producing) enzymatic processes.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Evert C Duin et al.
Methods in enzymology, 494, 159-187 (2011-03-16)
Methyl-coenzyme M reductase catalyzes the reversible synthesis of methane from methyl-coenzyme M in methanogenic and ANME-1 and ANME-2 Archaea. The purification procedure for methyl-coenzyme M reductase from Methanothermobacter marburgensis is described. The procedure is an accumulation of almost 30 years
R Hedderich et al.
European journal of biochemistry, 193(1), 255-261 (1990-10-05)
The reduction of the heterodisulfide of coenzyme M (H-S-CoM) and 7-mercaptoheptanoyl-L-threonine phosphate (H-S-HTP) is a key reaction in the metabolism of methanogenic bacteria. The heterodisulfide reductase catalyzing this step was purified 80-fold to apparent homogeneity from Methanobacterium thermoautotrophicum. The native
S Peinemann et al.
European journal of biochemistry, 186(1-2), 175-180 (1989-12-08)
Methanogenesis from methyl-CoM and H2, as catalyzed by inside-out vesicle preparations of the methanogenenic bacterium strain Gö1, was associated with ATP synthesis. That this ATP synthesis proceeded via an uncoupler-sensitive transmembrane proton gradient was concluded from the following results: 1.
B Solow et al.
Archives of biochemistry and biophysics, 345(2), 299-304 (1997-10-06)
The biochemical mechanism for the formation of the amide bond in N-(7-mercaptoheptanoyl)-L-threonine phosphate (HS-HTP) has been studied by measuring the incorporation of L-[3-(3)H]threonine into N-(7-mercaptoheptanoyl)-L-threonine (HS-HT) by cell extracts (CE) of Methanosarcina thermophila incubated with different precursors. Synthesis of HS-HT
Mishtu Dey et al.
Biochemistry, 49(51), 10902-10911 (2010-11-26)
Methyl-coenzyme M reductase (MCR) from methanogenic archaea catalyzes the terminal step in methanogenesis using coenzyme B (CoBSH) as the two-electron donor to reduce methyl-coenzyme M (methyl-SCoM) to form methane and the heterodisulfide, CoBS-SCoM. The active site of MCR contains an
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