Evidence map›Paper›PMID 21278279›Full record

ArticleApplied and environmental microbiology2011

Poly-alpha-glutamic acid synthesis using a novel catalytic activity of RimK from Escherichia coli K-12.

Kuniki Kino, Toshinobu Arai, Yasuhiro Arimura

Abstract read
In one paragraph

Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. A posttranslational modification of fimbriae drives pathogenicity inProceedings of the National Academy of Sciences of the United States of America · 2026
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  12. Systematic analysis of lysine malonylation inFrontiers in cellular and infection microbiology · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Diamine Biosynthesis: Research Progress and Application Prospects.Applied and environmental microbiology · 2020
    Review
  18. Article
  19. Review
  20. Structural polymorphism of the Escherichia coli poly-α-L-glutamate synthetase RimK.Acta crystallographica. Section F, Structural biology communications · 2018
    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

3 authors at 1 institution in 1 country.

Kuniki KinoDepartment of Applied Chemistry, Faculty of Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, Tokyo 169-8555, Japan. kkino@waseda.jp
Toshinobu Arai
Yasuhiro Arimura
Waseda University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly-L-α-amino acids have various applications because of their biodegradable properties and biocompatibility. Microorganisms contain several enzymes that catalyze the polymerization of L-amino acids in an ATP-dependent manner, but the products from these reactions contain amide linkages at the side residues of amino acids: e.g., poly-γ-glutamic acid, poly-ε-lysine, and cyanophycin. In this study, we found a novel catalytic activity of RimK, a ribosomal protein S6-modifying enzyme derived from Escherichia coli K-12. This enzyme catalyzed poly-α-glutamic acid synthesis from unprotected L-glutamic acid (Glu) by hydrolyzing ATP to ADP and phosphate. RimK synthesized poly-α-glutamic acid of various lengths; matrix-assisted laser desorption ionization-time of flight-mass spectrometry showed that a 46-mer of Glu (maximum length) was synthesized at pH 9. Interestingly, the lengths of polymers changed with changing pH. RimK also exhibited 86% activity after incubation at 55°C for 15 min, thus showing thermal stability. Furthermore, peptide elongation seemed to be catalyzed at the C terminus in a stepwise manner. Although RimK showed strict substrate specificity toward Glu, it also used, to a small extent, other amino acids as C-terminal substrates and synthesized heteropeptides. In addition, RimK-catalyzed modification of ribosomal protein S6 was confirmed. The number of Glu residues added to the protein varied with pH and was largest at pH 9.5.

Indexed as

CatalysisEscherichia coli K12Escherichia coli ProteinsGlutamic AcidHydrogen-Ion ConcentrationMagnetic Resonance SpectroscopyMolecular Sequence DataPeptidesPolylysineSpectrometry, Mass, Electrospray IonizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationEscherichia coli ProteinsGlutamic AcidPeptidesPolylysine

Identifiers

PMID21278279
PMCPMC3067337
OpenAlexW2132868339

What OpenQuestion holds

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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.