Evidence map›Paper›PMID 42817572›Full record

ArticleMicrobial biotechnology2026

Structural and Functional Characterisation of a Metagenome-Derived CYP108D18 Reveals an Unusual Dioxygen-Bound State and Selective Hydrocarbon Hydroxylation.

Simran Kundral, Peter D Giang, Alicia M Kirk, Julia B Buczynski, Kasun S A Arachchige, Sunil K Khare, Paul V Bernhardt, Paul N Evans, Luke W Guddat, Stephen G Bell and 1 more

Abstract read
In one paragraph

Article in Microbial biotechnology, 2026. 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
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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.

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

11 authors.

Simran KundralThe University of Queensland - Indian Institute of Technology Delhi (UQIITD) Research Academy, New Delhi, India.ORCID https://orcid.org/0000-0002-4225-9016
Peter D GiangSchool of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, Australia.ORCID https://orcid.org/0000-0002-1408-997X
Alicia M KirkSchool of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, Australia.ORCID https://orcid.org/0000-0002-2611-5274
Julia B BuczynskiSchool of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, Australia.ORCID https://orcid.org/0009-0000-9753-7207
Kasun S A ArachchigeCentre for Microscopy and Microanalysis, The University of Queensland, St. Lucia, Queensland, Australia.ORCID https://orcid.org/0000-0002-2169-2718
Sunil K KhareEnzyme and Microbial Biochemistry Laboratory, Department of Chemistry, Indian Institute of Technology Delhi, New Delhi, India.ORCID https://orcid.org/0000-0002-7339-3058
Paul V BernhardtSchool of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, Australia.ORCID https://orcid.org/0000-0001-6839-1763
Paul N EvansAustralian Centre for Ecogenomics, School of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, Australia.ORCID https://orcid.org/0000-0001-5995-2602
Luke W GuddatSchool of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, Australia.ORCID https://orcid.org/0000-0002-8204-8408
Stephen G BellSchool of Physics, Chemistry and Earth Sciences, Adelaide University, Adelaide, South Australia, Australia.ORCID https://orcid.org/0000-0002-7457-9727
James J De VossSchool of Chemistry and Molecular Biosciences, The University of Queensland, St Lucia, Queensland, Australia.ORCID https://orcid.org/0000-0002-2659-5140

Funding

Australian Research Council DP210103970
6 · The paper itself

Abstract

Cytochrome P450 enzymes form a large superfamily of monooxygenases capable of oxidising diverse substrates. Among them, members of the CYP108 family are recognised for their role in monoterpenoid oxidation. In this study, we report the identification and characterisation of a new CYP108 family member, CYP108D18, from a metagenome-assembled genome derived from microbial communities in a geothermal hot spring located in northern Queensland, Australia. Taxonomic binning associated CYP108D18 with a Novosphingobium species, a genus well-known for its bioremediation potential. CYP108D18 was heterologously expressed in Escherichia coli, yielding 640 nmol L

Indexed as

Cytochrome P-450 Enzyme SystemMetagenomeOxygenSphingomonadaceaeAustraliaCloning, MolecularEnzyme StabilityEscherichia coliGene ExpressionHot SpringsHydroxylationMolecular Docking SimulationMonoterpenesProtein BindingRecombinant ProteinsSubstrate SpecificityCytochrome P-450 Enzyme SystemMonoterpenesOxygenRecombinant Proteins

Identifiers

PMID42817572
PMCPMC13627977

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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.