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1 es for other methanogenic substrates such as monomethylamine.
4 rimethylamine-grown cell extracts to convert monomethylamine and dimethylamine to methyl-CoM was lost
7 nesis from trimethylamine, dimethylamine, or monomethylamine by various Methanosarcina species posses
8 in which different proteins of the resolved monomethylamine:coenzyme M methyl transfer reaction repl
9 was achieved with three purified proteins: a monomethylamine corrinoid protein (MMCP), the "A" isozym
13 itional novel features are the presence of a monomethylamine:corrinoid methyltransferase, the first t
14 or corrinoid protein for methanogenesis from monomethylamine detectable in extracts and that it inter
16 ansferases initiating methane formation from monomethylamine, dimethylamine, or trimethylamine, respe
18 monomethylamine, a 52-kDa polypeptide termed monomethylamine methyltransferase (MMAMT) methylates the
19 (MT2-A), and a newly isolated protein termed monomethylamine methyltransferase (MMAMT).MMAMT is a 170
21 Wild-type cells, but not DeltappylT, have monomethylamine methyltransferase activity during growth
22 located near a cluster of genes required for monomethylamine methyltransferase activity, including Mt
23 ol and methylamines with wild-type levels of monomethylamine methyltransferase and aminoacyl-tRNA(Pyl
24 Methanosarcina barkeri mtmB1 gene, encoding monomethylamine methyltransferase MtmB1, was introduced
27 cid, was found in the Methanosarcina barkeri monomethylamine methyltransferase protein in a position
29 xpressed with mtmB1, encoding the methanogen monomethylamine methyltransferase, UAG was translated as
30 sK and mtmB transcripts, encoding LysRS1 and monomethylamine methyltransferase, were detectable in Me
32 mtbA gene was required for dimethylamine and monomethylamine (MMA) utilization and was important, but
33 e was determined for a basic probe molecule, monomethylamine (MMA), bound at the minority Lewis acid
35 nesis from trimethylamine, dimethylamine and monomethylamine possess a novel residue, pyrrolysine.
37 ability of some microbial species to oxidize monomethylamine via glutamate-mediated pathways was prop
38 vitro reconstitution of CoM methylation with monomethylamine was achieved with three purified protein
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