Evidence map›Paper›PMID 12408752›Full record

ArticleThe Biochemical journal2003

Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin in Bacillus megaterium.

Evelyne Raux, Helen K Leech, Richard Beck, Heidi L Schubert, Patricio J Santander, Charles A Roessner, A Ian Scott, Jan H Martens, Dieter Jahn, Claude Thermes and 2 more

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

38 citing papers in PubMed, 106 citations in OpenAlex.

  1. Review
  2. Review
  3. Metabolic engineering ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Microbiology (Reading, England) · 2021
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. The requirement for cobalt in vitamin BBiochimica et biophysica acta. Molecular cell research · 2021
    Review
  14. Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020
    Review
  15. Inactivation ofJournal of bacteriology · 2019
    Article
  16. Article
  17. Article
  18. Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  19. Article
  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

12 authors at 2 institutions in 2 countries.

Evelyne RauxSchool of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, UK.
Helen K Leech
Richard Beck
Heidi L Schubert
Patricio J Santander
Charles A Roessner
A Ian Scott
Jan H Martens
Dieter Jahn
Claude Thermes
Alain Rambach
Martin J Warren
Technische Universität Braunschweig · DECentre de Génétique Moléculaire · FR

Funding

PORPHYRIN &CORRINOID BIOSYNTHESISR01DK032034 · NIDDK · TEXAS A&M UNIVERSITY SYSTEM · PI RAUSHEL, FRANK M. · 1986 to 2008
$1.0M
NIDDK NIH HHS 2 R01 DK32034-18
6 · The paper itself

Abstract

In Bacillus megaterium, the hemAXBCDL genes were isolated and were found to be highly similar to the genes from Bacillus subtilis that are required for the conversion of glutamyl-tRNA into uroporphyrinogen III. Overproduction and purification of HemC (porphobilinogen deaminase) and -D (uroporphyrinogen III synthase) allowed these enzymes to be used for the in vitro synthesis of uroporphyrinogen III from porphobilinogen. A second smaller cluster of three genes (termed sirABC) was also isolated and found to encode the enzymes that catalyse the transformation of uroporphyrinogen III into sirohaem on the basis of their ability to complement a defined Escherichia coli (cysG) mutant. The functions of SirC and -B were investigated by direct enzyme assay, where SirC was found to act as a precorrin-2 dehydrogenase, generating sirohydrochlorin, and SirB was found to act as a ferrochelatase responsible for the final step in sirohaem synthesis. CbiX, a protein found encoded within the main B. megaterium cobalamin biosynthetic operon, shares a high degree of similarity with SirB and acts as the cobaltochelatase associated with cobalamin biosynthesis by inserting cobalt into sirohydrochlorin. CbiX contains an unusual histidine-rich region in the C-terminal portion of the protein, which was not found to be essential in the chelation process. Sequence alignments suggest that SirB and CbiX share a similar active site to the cobaltochelatase, CbiK, from Salmonella enterica.

Indexed as

Amino Acid SequenceBacillus megateriumEscherichia coliHemeMethyltransferasesMolecular Sequence DataSalmonella typhimuriumUroporphyrinsVitamin B 1215,23-dihydrosirohydrochlorinHemeMethyltransferasessirohemeuroporphyrin-III C-methyltransferaseUroporphyrinsVitamin B 12

Identifiers

PMID12408752
PMCPMC1223173
OpenAlexW2034615318

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.