Ellermann, Joachim published the artcileMethyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum (strain Marburg). Purity, activity and novel inhibitors, Category: bromides-buliding-blocks, the publication is European Journal of Biochemistry (1989), 184(1), 63-8, database is CAplus and MEDLINE.
Methyl-coenzyme-M reductase from M. thermoautotrophicum (strain Marburg) was purified to a stage where, besides the α, β and γ subunits, no addnl. polypeptides were detectable in the preparation Under appropriate conditions the enzyme was found to catalyze the reduction of methyl-CoM with 7-mercaptoheptanoylthreonine phosphate (H-S-HTP) to CH4 at a specific rate of 2.5 μmol min-1 mg protein-1. This finding contradicts a recent report that methyl-CoM reductase is only active when some contaminating proteins are present. The 2 polypeptides encoded by the open reading frames ORF1 and ORF2 of the methyl-CoM reductase transcription unit did not copurify with the α, β and γ subunits. They were neither required nor did they stimulate the activity under the assay conditions. 3-Bromopropanesulfonate (apparent Ki = 0.05 μM) and 2-azidoethanesulfonate (apparent Ki = 1 μM) were found to be 2 new competitive inhibitors of methyl-CoM reductase. Both inhibitors were considerably more effective than the classical 2-bromoethanesulfonate (apparent Ki = 4 μM).
European Journal of Biochemistry published new progress about 55788-44-8. 55788-44-8 belongs to bromides-buliding-blocks, auxiliary class Bromide,Salt,Aliphatic hydrocarbon chain,Aliphatic hydrocarbon chain, name is Sodium 3-bromopropane-1-sulfonate, and the molecular formula is C3H6BrNaO3S, Category: bromides-buliding-blocks.
Referemce:
https://en.wikipedia.org/wiki/Bromide,
bromide – Wiktionary