Evidence map›Paper›PMID 26441143›Full record

ArticleACS chemical biology2015

Bacterial Genome Mining of Enzymatic Tools for Alkyne Biosynthesis.

Xuejun Zhu, Michael Su, Kadhirvel Manickam, Wenjun Zhang

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Biosynthesis of Isonitrile- and Alkyne-Containing Natural Products.Annual review of chemical and biomolecular engineering · 2022
    Review
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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

4 authors at 1 institution in 1 country.

Xuejun Zhu
Michael Su
Kadhirvel Manickam
Wenjun ZhangPhysical Biosciences Division, Lawrence Berkeley National Laboratory , Berkeley, California 94720, United States.
Lawrence Berkeley National Laboratory · US

Funding

In Situ Natural Product Labeling and ApplicationsDP2AT009148 · NCCIH · UNIVERSITY OF CALIFORNIA BERKELEY · PI ZHANG, WENJUN · 2015 to 2020
$2.8M
NCCIH NIH HHS DP2 AT009148NCCIH NIH HHS DP2AT009148
6 · The paper itself

Abstract

The alkyne is an important functionality widely used in material science, pharmaceutical science, and chemical biology, but the importance of this functionality is contrasted by the very limited number of enzymes known to be involved in alkyne biosynthesis. We recently reported the first known carrier protein-dependent pathway for terminal alkyne formation, and in silico analysis suggested that this mechanism could be widespread in bacteria. In this paper, we screened additional homologous gene cassettes presumed to be involved in alkyne biosynthesis using both in vitro biochemical study and an E. coli-polyketide synthase (PKS) reporting system for in vivo analysis. We discovered and characterized a new terminal alkyne biosynthetic pathway comprised of TtuA, -B, and -C from Teredinibacter turnerae T7901. While the acyl-CoA ligase homologue (TtuA) demonstrated promiscuity in the activation and loading of medium-chain fatty acids onto the carrier protein (TtuC), the desaturase homologue (TtuB) showed stringent substrate specificity toward C10 fatty acyl moieties. In addition, TtuB was demonstrated to be a bifunctional desaturase/acetylenase that efficiently catalyzed two sequential O2-dependent dehydrogenation reactions. A novel terminal-alkyne bearing polyketide was further produced upon coexpression of ttuABC and a PKS gene in E. coli. The discovery and characterization of TtuA, -B, and -C provides us with a new bifunctional desaturase/acetylenase for mechanistic and structural study and expands the scarce enzyme inventory for the biosynthesis of the alkyne functionality, which has important applications in synthetic and chemical biology.

Indexed as

AlkynesAmino Acid SequenceBiological AssayEscherichia coliGenetic TestingGenome, BacterialMolecular StructureMultigene FamilyPhylogenyPolyketide SynthasesSubstrate SpecificityAlkynesPolyketide Synthases

Identifiers

PMID26441143
PMCPMC4684755
OpenAlexW2413203161

What OpenQuestion holds

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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.