Evidence map›Paper›PMID 29432141›Full record

ReviewBiochemical Society transactions2018

Structure and function of the cytochrome P450 peroxygenase enzymes.

Andrew W Munro, Kirsty J McLean, Job L Grant, Thomas M Makris

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
22.6field-weighted citation impact, top 1% 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

66 citing papers in PubMed, 215 citations in OpenAlex.

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6 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 2 countries.

Andrew W MunroManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, 131 Princess Street, Manchester M1 7DN, U.K. andrew.munro@manchester.ac.uk.
Kirsty J McLeanManchester Institute of Biotechnology, School of Chemistry, The University of Manchester, 131 Princess Street, Manchester M1 7DN, U.K.
Job L GrantDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, U.S.A.
Thomas M MakrisDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, U.S.A.
University of Manchester · GBUniversity of South Carolina · US

Funding

Biotechnology and Biological Sciences Research Council BB/M017702/1Biotechnology and Biological Sciences Research Council BB/N006275/1
6 · The paper itself

Abstract

The cytochromes P450 (P450s or CYPs) constitute a large heme enzyme superfamily, members of which catalyze the oxidative transformation of a wide range of organic substrates, and whose functions are crucial to xenobiotic metabolism and steroid transformation in humans and other organisms. The P450 peroxygenases are a subgroup of the P450s that have evolved in microbes to catalyze the oxidative metabolism of fatty acids, using hydrogen peroxide as an oxidant rather than NAD(P)H-driven redox partner systems typical of the vast majority of other characterized P450 enzymes. Early members of the peroxygenase (CYP152) family were shown to catalyze hydroxylation at the α and β carbons of medium-to-long-chain fatty acids. However, more recent studies on other CYP152 family P450s revealed the ability to oxidatively decarboxylate fatty acids, generating terminal alkenes with potential applications as drop-in biofuels. Other research has revealed their capacity to decarboxylate and to desaturate hydroxylated fatty acids to form novel products. Structural data have revealed a common active site motif for the binding of the substrate carboxylate group in the peroxygenases, and mechanistic and transient kinetic analyses have demonstrated the formation of reactive iron-oxo species (compounds I and II) that are ultimately responsible for hydroxylation and decarboxylation of fatty acids, respectively. This short review will focus on the biochemical properties of the P450 peroxygenases and on their biotechnological applications with respect to production of volatile alkenes as biofuels, as well as other fine chemicals.

Indexed as

Amino Acid SequenceBiofuelsCarboxylic AcidsCatalysisCatalytic DomainCytochrome P-450 Enzyme SystemFatty AcidsHumansHydrogen PeroxideHydroxylationOxidation-ReductionPeroxidasesStructure-Activity RelationshipSubstrate SpecificityBiofuelsCarboxylic AcidsCytochrome P-450 Enzyme Systemcytochrome P-450 peroxygenaseFatty AcidsHydrogen PeroxidePeroxidasesalkenescytochrome P450enzyme mechanismiron-oxo speciesperoxygenasesubstrate decarboxylation

Identifiers

PMID29432141
PMCPMC5818669
OpenAlexW2779315858

What OpenQuestion holds

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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.