Evidence map›Paper›PMID 17827296›Full record

ArticleJournal of bacteriology2007

The CbiB protein of Salmonella enterica is an integral membrane protein involved in the last step of the de novo corrin ring biosynthetic pathway.

Carmen L Zayas, Kathy Claas, Jorge C Escalante-Semerena

Abstract read
In one paragraph

Article in Journal of bacteriology, 2007. 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
0.8field-weighted citation impact, top 28% 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, 32 citations in OpenAlex.

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  8. The requirement for cobalt in vitamin BBiochimica et biophysica acta. Molecular cell research · 2021
    Review
  9. Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020
    Review
  10. Article
  11. Article
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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

3 authors at 1 institution in 1 country.

Carmen L ZayasDepartment of Bacteriology, University of Wisconsin-Madison, WI 53706, USA.
Kathy Claas
Jorge C Escalante-Semerena
University 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
B12 Biosysthesis and Anaerobic Metabolism in SalmonellaR01GM040313 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ESCALANTE, JORGE C · 1988 to 2009
$3.0M
Biochemistry and Genetics of Corrin Ring BiosynthesisF31GM064009 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ZAYAS, CARMEN L · 2001 to 2006
$199k
NIGMS NIH HHS F31 GM064009NIGMS NIH HHS F31-GM64009NIGMS NIH HHS GM40313NIGMS NIH HHS R01 GM040313NIGMS NIH HHS R37 GM040313
6 · The paper itself

Abstract

We report results of studies of the conversion of adenosylcobyric acid (AdoCby) to adenosylcobinamide-phosphate, the last step of the de novo corrin ring biosynthetic branch of the adenosylcobalamin (coenzyme B12) pathway of Salmonella enterica serovar Typhimurium LT2. Previous reports have implicated the CbiB protein in this step of the pathway. Hydropathy analysis predicted that CbiB would be an integral membrane protein. We used a computer-generated topology model of the primary sequence of CbiB to guide the construction of CbiB-LacZ and CbiB-PhoA protein fusions, which were used to explore the general topology of CbiB in the cell membrane. A refined model of CbiB as an integral membrane protein is presented. In vivo analyses of the effect of single-amino-acid changes showed that periplasm- and cytosol-exposed residues are critical for CbiB function. Results of in vivo studies also show that ethanolamine-phosphate (EA-P) is a substrate of CbiB, but l-Thr-P is not, and that CbiB likely activates AdoCby by phosphorylation. The latter observation leads us to suggest that CbiB is a synthetase not a synthase enzyme. Results from mass spectrometry and bioassay experiments indicate that serovar Typhimurium synthesizes norcobalamin (cobalamin lacking the methyl group at C176) when EA-P is the substrate of CbiB.

Indexed as

Amino Acid SequenceArchaeal ProteinsBacterial ProteinsConserved SequenceCorrinoidsDNA PrimersKineticsMembrane ProteinsModels, MolecularMolecular Sequence DataPlasmidsProtein ConformationRecombinant ProteinsSalmonella entericaSalmonella typhimuriumSequence AlignmentArchaeal ProteinsBacterial ProteinscorrinCorrinoidsDNA PrimersMembrane ProteinsRecombinant Proteins

Identifiers

PMID17827296
PMCPMC2168724
OpenAlexW2105241978

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.