Evidence map›Paper›PMID 38942512›Full record

ArticleMethods in enzymology2024

Characterization of UbiA terpene synthases with a precursor overproduction system in Escherichia coli.

Tyler A Alsup, Melvin Osei Opoku, Jeffrey D Rudolf

Abstract read
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In one paragraph

Article in Methods in enzymology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
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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.

Tyler A AlsupDepartment of Chemistry, University of Florida, Gainesville, FL, United States.
Melvin Osei OpokuDepartment of Chemistry, University of Florida, Gainesville, FL, United States.
Jeffrey D RudolfDepartment of Chemistry, University of Florida, Gainesville, FL, United States. Electronic address: jrudolf@chem.ufl.edu.

Funding

Discovery and Biosynthesis of Bacterial TerpenoidsR35GM142574 · NIGMS · UNIVERSITY OF FLORIDA · PI Jeffrey Daniel Rudolf · 2021 to 2026
$2.4M
Chemistry-Biology Interface Training Program at the University of FloridaT32GM136583 · NIGMS · UNIVERSITY OF FLORIDA · PI Chenglong Li · 2020 to 2026
$1.1M
Acquisition of a Q Exactive HF Hybrid Quadrupole-OrbitrapS10OD021758 · OD · UNIVERSITY OF FLORIDA · PI BASSO, KARI B · 2017 to 2017
$600k
NIGMS NIH HHS R35 GM142574NIGMS NIH HHS T32 GM136583NIH HHS S10 OD021758US Department of Energy DE-AC02-05CH11231
6 · The paper itself

Abstract

Expression and purification of membrane-bound proteins remains a challenge and limits enzymology efforts, contributing to a substantial knowledge gap in the biochemical functions of many proteins found in nature. Accordingly, the study of bacterial UbiA terpene synthases (TSs) has been limited due to the experimental hurdles required to purify active enzymes for characterization in vitro. Previous work employed the use of microsomes or crude membrane fractions to test enzyme activity; however, these methods can be labor intensive, require access to an ultracentrifuge, or may not be suitable for all membrane-bound TSs. We detail here an alternative strategy for the in vivo expression and biochemical characterization of the membrane associated UbiA TSs by employing a precursor overproduction system in Escherichia coli.

Indexed as

Alkyl and Aryl TransferasesEscherichia coliBacterial ProteinsRecombinant ProteinsAlkyl and Aryl TransferasesBacterial ProteinsRecombinant Proteinsterpene synthaseBacteriaBiosynthesisMembrane proteinNatural productTerpene synthaseUbiA

Identifiers

PMID38942512
PMCPMC11216710

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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.