Evidence map›Paper›PMID 31410607›Full record

ArticleAMB Express2019

Identification and characterization of levulinyl-CoA synthetase from Pseudomonas citronellolis, which differs phylogenetically from LvaE of Pseudomonas putida.

Hiroshi Habe, Hideaki Koike, Yuya Sato, Yosuke Iimura, Tomoyuki Hori, Manabu Kanno, Nobutada Kimura, Kohtaro Kirimura

Open access · goldAbstract read
In one paragraph

Article in AMB Express, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 53% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

8 authors at 2 institutions in 1 country.

Hiroshi HabeEnvironmental Management Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba West, 16-1 Onogawa, Tsukuba, Ibaraki, 305-8569, Japan. hiroshi.habe@aist.go.jp.ORCID http://orcid.org/0000-0001-8721-2206
Hideaki KoikeBioproduction Research Institute, AIST, Tsukuba Central 6-10, 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8566, Japan.
Yuya SatoEnvironmental Management Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba West, 16-1 Onogawa, Tsukuba, Ibaraki, 305-8569, Japan.
Yosuke IimuraEnvironmental Management Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba West, 16-1 Onogawa, Tsukuba, Ibaraki, 305-8569, Japan.
Tomoyuki HoriEnvironmental Management Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba West, 16-1 Onogawa, Tsukuba, Ibaraki, 305-8569, Japan.
Manabu KannoBioproduction Research Institute, AIST, Tsukuba Central 6-10, 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8566, Japan.
Nobutada KimuraBioproduction Research Institute, AIST, Tsukuba Central 6-10, 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8566, Japan.
Kohtaro KirimuraDepartment of Applied Chemistry, Faculty of Science and Engineering, Waseda University, Tokyo, 169-8555, Japan.
National Institute of Advanced Industrial Science and Technology · JPWaseda University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Levulinic acid (LA) is a building block alternative to fermentable sugars derived from cellulosic biomass. Among LA catabolic processes in Pseudomonas putida KT2440, ligation of coenzyme A (CoA) to LA by levulinyl-CoA synthetase (LvaE) is known to be an initial enzymatic step in LA metabolism. To identify the genes involved in the first step of LA metabolism in Pseudomonas citronellolis LA18T, RNA-seq-based comparative transcriptome analysis was carried out for LA18T cells during growth on LA and pyruvic acid. The two most highly upregulated genes with LA exhibited amino acid sequence homologies to cation acetate symporter and 5-aminolevulinic acid dehydratase from Pseudomonas spp. Potential LA metabolic genes (lva genes) in LA18T that clustered with these two genes and were homologous to lva genes in KT2440 were identified, including lvaE2 of LA18T, which exhibited 35% identity with lvaE of KT2440. Using Escherichia coli cells with the pCold™ expression system, LvaE2 was produced and investigated for its activity toward LA. High performance liquid chromatography analysis confirmed that crude extracts of E. coli cells expressing the lvaE2 gene could convert LA to levulinyl-CoA in the presence of both HS-CoA and ATP. Phylogenetic analysis revealed that LvaE2 and LvaE formed a cluster with medium-chain fatty acid CoA synthetase, but they fell on different branches. Superimposition of LvaE2 and LvaE homology-based model structures suggested that LvaE2 had a larger tunnel for accepting fatty acid substrates than LvaE. These results indicate that LvaE2 is a novel levulinyl-CoA synthetase.

Indexed as

Acyl-CoA synthetaseLevulinic acidLevulinyl-CoA synthetaseLignocellulosePseudomonas citronellolis

Identifiers

PMID31410607
PMCPMC6692424
OpenAlexW2968003836

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.