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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L G Bonacker et al.
European journal of biochemistry, 217(2), 587-595 (1993-10-15)
Methyl-coenzyme M reductase (MCR) catalyses the methane-forming step in the energy metabolism of methanogenic Archaea. It brings about the reduction of methyl-coenzyme M (CH3-S-CoM) by 7-mercaptoheptanoylthreonine phosphate (H-S-HTP). Methanobacterium thermoautotrophicum contains two isoenzymes of MCR, designated MCR I and MCR
K D Olson et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(10), 4099-4103 (1991-05-15)
Inactive 2-(methylthio)ethanesulfonic acid (CH3-S-CoM) reductase was partially activated by exposure to light. This simplified system replaces the complex enzymatic system of protein components A2, A3a, A3b, and ATP, which previously represented the only available means of reactivating the enzyme. Components
U Ermler et al.
Science (New York, N.Y.), 278(5342), 1457-1462 (1997-12-31)
Methyl-coenzyme M reductase (MCR), the enzyme responsible for the microbial formation of methane, is a 300-kilodalton protein organized as a hexamer in an alpha2beta2gamma2 arrangement. The crystal structure of the enzyme from Methanobacterium thermoautotrophicum, determined at 1.45 angstrom resolution for
P E Rouvière et al.
Journal of bacteriology, 170(9), 3946-3952 (1988-09-01)
When titanium(III) citrate was used as electron donor for the reduction of methyl coenzyme M by the methyl coenzyme M methylreductase system of Methanobacterium thermoautotrophicum delta H, component A1 was no longer required. The simpler system thus obtained required components
D A Grahame et al.
Biochemical and biophysical research communications, 147(1), 254-258 (1987-08-31)
Buffer-soluble extracts of acetate-grown Methanosarcina barkeri catalyzed methanogenesis from acetate in the presence of hydrogen and ATP. The rates of methane formation from either acetate plus ATP, or acetylphosphate without ATP added, were approximately doubled by the addition of coenzyme
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