Evidence map›Paper›PMID 20677021›Full record

ReviewApplied microbiology and biotechnology2010

Multiple roles of ATP:cob(I)alamin adenosyltransferases in the conversion of B12 to coenzyme B12.

Paola E Mera, Jorge C Escalante-Semerena

Open access · greenAbstract readReview
In one paragraph

Review in Applied microbiology and biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Visualization of a radical B12 enzyme with its G-protein chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Light-dependent gene regulation by a coenzyme B12-based photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

2 authors at 2 institutions in 1 country.

Paola E MeraDepartment of Developmental Biology, Stanford University, 279 Campus Drive, Stanford, CA 94305, USA.
Jorge C Escalante-Semerena
Stanford University · USUniversity of Wisconsin–Madison · US

Funding

Request for a supplement for equipmentR37GM040313 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ESCALANTE, JORGE C · 2010 to 2018
$3.5M
NIGMS NIH HHS R37 GM040313NIGMS NIH HHS R37 GM40313
6 · The paper itself

Abstract

Our mechanistic understanding of the conversion of vitamin B(12) into coenzyme B(12) (a.k.a. adenosylcobalamin, AdoCbl) has been substantially advanced in recent years. Insights into the multiple roles played by ATP:cob(I)alamin adenosyltransferase (ACA) enzymes have emerged through the crystallographic, spectroscopic, biochemical, and mutational analyses of wild-type and variant proteins. ACA enzymes circumvent the thermodynamic barrier posed by the very low redox potential associated with the reduction of cob(II)alamin to cob(I)alamin by generating a unique four-coordinate cob(II)alamin intermediate that is readily converted to cob(I)alamin by physiological reductants. ACA enzymes not only synthesize AdoCbl but also they deliver it to the enzymes that use it, and in some cases, enzymes in which its function is needed to maintain the fidelity of the AdoCbl delivery process have been identified. Advances in our understanding of ACA enzyme function have provided valuable insights into the role of specific residues, and into why substitutions of these residues have profound negative effects on human health. From an applied science standpoint, a better understanding of the adenosylation reaction may lead to more efficient ways of synthesizing AdoCbl.

Indexed as

Adenosine TriphosphateAlkyl and Aryl TransferasesCobamidesVitamin B 12Adenosine TriphosphateAlkyl and Aryl TransferasescobamamideCobamidescob(I)alamin adenosyltransferaseVitamin B 12

Identifiers

PMID20677021
PMCPMC3034633
OpenAlexW2086119565

What OpenQuestion holds

Textmetadata
LicenceTDM
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.