Evidence map›Paper›PMID 28892347›Full record

ArticleACS chemical biology2017

Two Cooperative Glycosyltransferases Are Responsible for the Sugar Diversity of Saquayamycins Isolated from Streptomyces sp. KY 40-1.

Shaimaa M Salem, Stevi Weidenbach, Jürgen Rohr

Abstract read
In one paragraph

Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

16 citing papers in PubMed, 36 citations in OpenAlex.

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  13. Efficient Multiplex Genome Editing inFrontiers in bioengineering and biotechnology · 2020
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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.

Shaimaa M SalemDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky , Lexington, Kentucky 40536, United States.ORCID 0000-0002-9149-5365
Stevi WeidenbachDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky , Lexington, Kentucky 40536, United States.ORCID 0000-0001-7994-4458
Jürgen RohrDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky , Lexington, Kentucky 40536, United States.ORCID 0000-0001-6447-5951
University of Kentucky · US

Funding

University of Kentucky Markey Cancer Center Support Grant ECIA SupplementP30CA177558 · NCI · UNIVERSITY OF KENTUCKY · PI Bernard Mark Evers · 2013 to 2026
$38.3M
SAMPLE COREU24DK097215 · NIDDK · UNIVERSITY OF KENTUCKY · PI FAN, TERESA WHEI-MEI, HIGASHI, RICHARD M · 2013 to 2017
$8.7M
NOVEL AUREOLIC ACID TYPE ANTITUMOR AGENTSR01CA091901 · NCI · UNIVERSITY OF KENTUCKY · PI ROHR, JURGEN T · 2001 to 2017
$3.6M
Exploring Post-Type II PKS Frame ModificationsR01GM105977 · NIGMS · UNIVERSITY OF KENTUCKY · PI ROHR, JURGEN T · 2014 to 2017
$1.1M
NCI NIH HHS P30 CA177558NCI NIH HHS R01 CA091901NIDDK NIH HHS U24 DK097215NIGMS NIH HHS R01 GM105977
6 · The paper itself

Abstract

Glycosyltransferases are key enzymes involved in the biosynthesis of valuable natural products providing an excellent drug-tailoring tool. Herein, we report the identification of two cooperative glycosyltransferases from the sqn gene cluster directing the biosynthesis of saquayamycins in Streptomyces sp. KY40-1: SqnG1 and SqnG2. Gene inactivation of sqnG1 leads to 50-fold decrease in saquayamycin production, while inactivation of sqnG2 leads to complete production loss, suggesting that SqnG2 acts as dual O- and C-glycosyltransferase. Gene inactivation of a third putative glycosyltransferase-encoding gene, sqnG3, does not affect saquayamycin production in a major way, suggesting that SqnG3 has no or a supportive role in glycosylation. The data indicate that SqnG1 and SqnG2 are solely and possibly cooperatively responsible for the sugar diversity observed in saquayamycins 1-7. This is the first evidence of a glycosyltransferase system showing codependence to achieve dual O- and C-glycosyltransferase activity, utilizing NDP-activated d-olivose, l-rhodinose, as well as an unusual amino sugar, presumably 3,6-dideoxy-l-idosamine.

Indexed as

AnthraquinonesCarbohydrate ConformationCarbohydratesGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicGlycosyltransferasesStreptomycesAnthraquinonesCarbohydratesGlycosyltransferases

Identifiers

PMID28892347
PMCPMC5886728
OpenAlexW2756247685

What OpenQuestion holds

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Registered trials

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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.