Evidence map›Paper›PMID 25313086›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase.

Tomislav Ticak, Duncan J Kountz, Kimberly E Girosky, Joseph A Krzycki, Donald J Ferguson

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.3field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 93 citations in OpenAlex.

  1. Trial
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  7. Methionine synthesis and glycine betaine demethylation are intricately intertwined in cosmopolitan marine bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Glycine betaine metabolism is enabled inApplied and environmental microbiology · 2024
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. WidespreadmLife · 2023
    Article
  18. Review
  19. Methyl-Based Methanogenesis: an Ecological and Genomic Review.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Tomislav TicakDepartment of Microbiology, Miami University, Oxford, OH 45056;
Duncan J KountzDepartment of Microbiology and.
Kimberly E GiroskyDepartment of Microbiology and.
Joseph A KrzyckiDepartment of Microbiology and Biochemistry Program, The Ohio State University, Columbus, OH 43210; and krzycki.1@osu.edu fergusdj@miamioh.edu.
Donald J FergusonDepartment of Microbiology, Miami University, Oxford, OH 45056; Miami University Hamilton, Hamilton, OH 45011 krzycki.1@osu.edu fergusdj@miamioh.edu.
Miami University · USCzech Academy of Sciences, Institute of Microbiology · CZThe Ohio State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

COG5598 comprises a large number of proteins related to MttB, the trimethylamine:corrinoid methyltransferase. MttB has a genetically encoded pyrrolysine residue proposed essential for catalysis. MttB is the only known trimethylamine methyltransferase, yet the great majority of members of COG5598 lack pyrrolysine, leaving the activity of these proteins an open question. Here, we describe the function of one of the nonpyrrolysine members of this large protein family. Three nonpyrrolysine MttB homologs are encoded in Desulfitobacterium hafniense, a Gram-positive strict anaerobe present in both the environment and human intestine. D. hafniense was found capable of growth on glycine betaine with electron acceptors such as nitrate or fumarate, producing dimethylglycine and CO2 as products. Examination of the genome revealed genes for tetrahydrofolate-linked oxidation of a methyl group originating from a methylated corrinoid protein, but no obvious means to carry out corrinoid methylation with glycine betaine. DSY3156, encoding one of the nonpyrrolysine MttB homologs, was up-regulated during growth on glycine betaine. The recombinant DSY3156 protein converts glycine betaine and cob(I)alamin to dimethylglycine and methylcobalamin. To our knowledge, DSY3156 is the first glycine betaine:corrinoid methyltransferase described, and a designation of MtgB is proposed. In addition, DSY3157, an adjacently encoded protein, was shown to be a methylcobalamin:tetrahydrofolate methyltransferase and is designated MtgA. Homologs of MtgB are widely distributed, especially in marine bacterioplankton and nitrogen-fixing plant symbionts. They are also found in multiple members of the human microbiome, and may play a beneficial role in trimethylamine homeostasis, which in recent years has been directly tied to human cardiovascular health.

Indexed as

BetaineChromatography, Thin LayerDesulfitobacteriumGenes, BacterialGlycine N-MethyltransferaseHumansLysineMethylaminesMethylationPhylogenyReal-Time Polymerase Chain ReactionBetaineGlycine N-MethyltransferaseLysineMethylaminespyrrolysinetrimethylamineCOG5598Desulfitobacterium hafnienseglycine betainel-pyrrolysinetrimethylamine methyltransferase

Identifiers

PMID25313086
PMCPMC4217433
OpenAlexW2029625739

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.