Evidence map›Paper›PMID 33176055›Full record

ArticleFEBS open bio2021

Characterization of a thermophilic cytochrome P450 of the CYP203A subfamily from Binh Chau hot spring in Vietnam.

Kim-Thoa Nguyen, Ngoc-Lan Nguyen, Mohammed Milhim, Van-Tung Nguyen, Thi-Hong-Nhung Lai, Huy-Hoang Nguyen, Thi-Thanh-Xuan Le, Thi-Tuyet-Minh Phan, Rita Bernhardt

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

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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

9 authors at 2 institutions in 2 countries.

Kim-Thoa NguyenInstitute of Biotechnology, Vietnam Academy of Science and Technology, Hanoi, Vietnam.ORCID 0000-0002-2702-1907
Ngoc-Lan NguyenGraduate University of Science and Technology, Vietnam Academy of Science and Technology, Hanoi, Vietnam.
Mohammed MilhimDepartment of Biochemistry, Saarland University, Saarbrucken, Germany.
Van-Tung NguyenGraduate University of Science and Technology, Vietnam Academy of Science and Technology, Hanoi, Vietnam.
Thi-Hong-Nhung LaiInstitute of Biotechnology, Vietnam Academy of Science and Technology, Hanoi, Vietnam.
Huy-Hoang NguyenGraduate University of Science and Technology, Vietnam Academy of Science and Technology, Hanoi, Vietnam.
Thi-Thanh-Xuan LeInstitute of Biotechnology, Vietnam Academy of Science and Technology, Hanoi, Vietnam.
Thi-Tuyet-Minh PhanInstitute of Biotechnology, Vietnam Academy of Science and Technology, Hanoi, Vietnam.
Rita BernhardtDepartment of Biochemistry, Saarland University, Saarbrucken, Germany.
Vietnam Academy of Science and Technology · VNSaarland University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochromes P450 (CYPs or P450s) comprise a superfamily of heme-containing monooxygenases that are involved in a variety of biological processes. CYPs have broad utilities in industry, but most exhibit low thermostability, limiting their use on an industrial scale. Highly thermostable enzymes can be obtained from thermophiles in geothermal areas, including hot springs, offshore oil-producing wells and volcanoes. Here, we report the identification of a gene encoding for a thermophilic CYP from the Binh Chau hot spring metagenomic database, which was designated as P450-T2. The deduced amino acid sequence showed the highest identity of 73.15% with CYP203A1 of Rhodopseudomonas palustris, supporting that P450-T2 is a member of the CYP203A subfamily. Recombinant protein expression yielded 541 nm. The optimal temperature and pH of P450-T2 were 50 °C and 8.0, respectively. The half-life of P450-T2 was 50.2 min at 50 °C, and its melting temperature was 56.80 ± 0.08 °C. It was found to accept electrons from all tested redox partners systems, with BmCPR-Fdx2 being the most effective partner. Screening for putative substrates revealed binding of phenolic compounds, such as l-mimosine and emodin, suggesting a potential application of this new thermophilic P450 in the production of the corresponding hydroxylated products.

Indexed as

MetagenomeAmino Acid SequenceBacterial ProteinsCytochrome P-450 Enzyme SystemEmodinHot SpringsMimosineRecombinant ProteinsRhodopseudomonasSequence Homology, Amino AcidSubstrate SpecificityVietnamBacterial ProteinsCytochrome P-450 Enzyme SystemEmodinMimosineRecombinant ProteinsBinh Chau hot springCYP203A subfamilycytochromeDNA metagenomeP450-T2thermophilic P450

Identifiers

PMID33176055
PMCPMC7780096
OpenAlexW3104460989

What OpenQuestion holds

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LicenceCC BY
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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.