Evidence map›Paper›PMID 21035730›Full record

ArticleChemistry & biology2010

N-acylation during glidobactin biosynthesis by the tridomain nonribosomal peptide synthetase module GlbF.

Heidi J Imker, Daniel Krahn, Jérôme Clerc, Markus Kaiser, Christopher T Walsh

Abstract read
In one paragraph

Article in Chemistry & biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
7.2field-weighted citation impact, top 3% 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

40 citing papers in PubMed, 86 citations in OpenAlex.

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  7. On the origin of amphi-enterobactin fragments produced by Vibrio campbellii species.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
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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

5 authors at 2 institutions in 2 countries.

Heidi J ImkerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
Daniel Krahn
Jérôme Clerc
Markus Kaiser
Christopher T Walsh
University of Duisburg-Essen · DEHarvard University · US

Funding

The Vancomycin Biosynthetic Assembly lineR01GM049338 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WALSH, CHRISTOPHER T · 1993 to 2012
$6.2M
NIGMS NIH HHS GM49338NIGMS NIH HHS R01 GM049338
6 · The paper itself

Abstract

Glidobactins are hybrid NRPS-PKS natural products that function as irreversible proteasome inhibitors. A variety of medium chain 2(E),4(E)-diene fatty acids N-acylate the peptidolactam core and contribute significantly to the potency of proteasome inhibition. We have expressed the initiation NRPS module GlbF (C-A-T) in Escherichia coli and observe soluble active protein only on coexpression with the 8 kDa MbtH-like protein, GlbE. Following adenylation and installation of Thr as a T-domain thioester, the starter condensation domain utilizes fatty acyl-CoA donors to acylate the Thr(1) amino group and generate the fatty acyl-Thr(1)-S-pantetheinyl-GlbF intermediate to be used in subsequent chain elongation. Previously proposed to be mediated via acyl carrier protein fatty acid donors, direct utilization of fatty acyl-CoA donors for N-acylation of T-domain tethered amino acids is likely a common strategy for chain initiation in NRPS-mediated lipopeptide biosynthesis.

Indexed as

AcylationAcyl Coenzyme ABacterial ProteinsBurkholderiaPeptides, CyclicPeptide SynthasesProtein Structure, TertiaryAcyl Coenzyme ABacterial Proteinsglidobactin Anon-ribosomal peptide synthasePeptides, CyclicPeptide Synthases

Identifiers

PMID21035730
PMCPMC3062200
OpenAlexW1967321353

What OpenQuestion holds

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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.