Evidence map›Paper›PMID 18772284›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2008

Getting a handle on the role of coenzyme M in alkene metabolism.

Arathi M Krishnakumar, Darius Sliwa, James A Endrizzi, Eric S Boyd, Scott A Ensign, John W Peters

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. The pathway for coenzyme M biosynthesis in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Ketone body metabolism and cardiovascular disease.American journal of physiology. Heart and circulatory physiology · 2013
    Review
  15. The Wolfe cycle comes full circle.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  16. Article
  17. Article
  18. Review
  19. 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

6 authors at 2 institutions in 1 country.

Arathi M KrishnakumarChemistry and Biochemistry Building, Montana State University, Bozeman, MT 59717, USA.
Darius Sliwa
James A Endrizzi
Eric S Boyd
Scott A Ensign
John W Peters
Montana State University · USUtah State University · US

Funding

Microbial metabolism of aliphatic alkenes &epoxidesR01GM051805 · NIGMS · UTAH STATE UNIVERSITY · PI ENSIGN, SCOTT A. · 2000 to 2008
$2.1M
MICROBIAL METABOLISM OF ALIPHATIC ALKENES AND EPOXIDESR29GM051805 · NIGMS · UTAH STATE UNIVERSITY · PI ENSIGN, SCOTT A. · 1995 to 1999
–
NIGMS NIH HHS R01 GM051805NIGMS NIH HHS R29 GM051805
6 · The paper itself

Abstract

Coenzyme M (2-mercaptoethanesulfonate; CoM) is one of several atypical cofactors discovered in methanogenic archaea which participate in the biological reduction of CO(2) to methane. Elegantly simple, CoM, so named for its role as a methyl carrier in all methanogenic archaea, is the smallest known organic cofactor. It was thought that this cofactor was used exclusively in methanogenesis until it was recently discovered that CoM is a key cofactor in the pathway of propylene metabolism in the gram-negative soil microorganism Xanthobacter autotrophicus Py2. A four-step pathway requiring CoM converts propylene and CO(2) to acetoacetate, which feeds into central metabolism. In this process, CoM is used to activate and convert highly electrophilic epoxypropane, formed from propylene epoxidation, into a nucleophilic species that undergoes carboxylation. The unique properties of CoM provide a chemical handle for orienting compounds for site-specific redox chemistry and stereospecific catalysis. The three-dimensional structures of several of the enzymes in the pathway of propylene metabolism in defined states have been determined, providing significant insights into both the enzyme mechanisms and the role of CoM in this pathway. These studies provide the structural basis for understanding the efficacy of CoM as a handle to direct organic substrate transformations at the active sites of enzymes.

Indexed as

AlkenesAmino Acid SequenceMesnaModels, MolecularMolecular Sequence DataStructure-Activity RelationshipXanthobacterAlkenesMesnapropylene

Identifiers

PMID18772284
PMCPMC2546864
OpenAlexW2106086136

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.