Evidence map›Paper›PMID 17526703›Full record

ArticleJournal of bacteriology2007

An anhydro-N-acetylmuramyl-L-alanine amidase with broad specificity tethered to the outer membrane of Escherichia coli.

Tsuyoshi Uehara, James T Park

Open access · greenAbstract 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 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.8field-weighted citation impact, top 6% 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, 85 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Outer Membrane Vesicles: Biogenesis, Functions, and Issues.Microbiology and molecular biology reviews : MMBR · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. The Tol-Pal system is required for peptidoglycan-cleaving enzymes to complete bacterial cell division.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. An amidase is required for proper intercellular communication in the filamentous cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2017
    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 1 institution in 1 country.

Tsuyoshi UeharaDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA. tsuyoshi.uehara@tufts.edu
James T Park
Tufts University · US

Funding

MUROPEPTIDE RECYCLING PATHWAY &BETA LACTAMASE INDUCTIONR01GM051610 · NIGMS · TUFTS UNIVERSITY BOSTON · PI PARK, JAMES T · 1996 to 2006
$975k
NIGMS NIH HHS GM51610NIGMS NIH HHS R01 GM051610
6 · The paper itself

Abstract

From its amino acid sequence homology with AmpD, we recognized YbjR, now renamed AmiD, as a possible second 1,6-anhydro-N-acetylmuramic acid (anhMurNAc)-l-alanine amidase in Escherichia coli. We have now confirmed that AmiD is an anhMurNAc-l-Ala amidase and demonstrated that AmpD and AmiD are the only enzymes present in E. coli that are able to cleave the anhMurNAc-l-Ala bond. The activity was present only in the outer membrane fraction obtained from an ampD mutant. In contrast to AmpD, which is specific for the anhMurNAc-l-alanine bond, AmiD also cleaved the bond between MurNAc and l-alanine in both muropeptides and murein sacculi. Unlike the periplasmic murein amidases, AmiD did not participate in cell separation. ampG mutants, which are unable to import GlcNAc-anhMurNAc-peptides into the cytoplasm, released mainly peptides into the medium due to AmiD activity, whereas an ampG amiD double mutant released a large amount of intact GlcNAc-anhMurNAc-peptides into the medium.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsGene DeletionMolecular Sequence DataMutationN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanSequence Homology, Amino AcidSubstrate SpecificityBacterial Outer Membrane ProteinsEscherichia coli ProteinsN-Acetylmuramoyl-L-alanine AmidasePeptidoglycan

Identifiers

PMID17526703
PMCPMC1951811
OpenAlexW2015213080

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.