Evidence map›Paper›PMID 30533540›Full record

ReviewSynthetic and systems biotechnology2018

Rational and semi-rational engineering of cytochrome P450s for biotechnological applications.

Lian-Hua Xu, Yi-Ling Du

Erratum issuedOpen access · goldAbstract readReview
In one paragraph

Review in Synthetic and systems biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 48 citations in OpenAlex.

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  10. Epoxyalcohol Synthase Branch of Lipoxygenase Cascade.Current issues in molecular biology · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Lian-Hua XuCollege of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China.
Yi-Ling DuInstitute of Pharmaceutical Biotechnology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
First Affiliated Hospital Zhejiang University · CNZhejiang Sci-Tech University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cytochrome P450 enzymes are ubiquitous heme-thiolate proteins performing regioselective and stereoselective oxygenation reactions in cellular metabolism. Due to their broad substrate scope and catalytic versatility, P450 enzymes are also attractive candidates for many industrial and biopharmaceutical applications. For particular uses, enzyme properties of P450s can be further optimized through directed evolution, rational, and semi-rational engineering approaches, all of which introduce mutations within the P450 structures. In this review, we describe the recent applications of these P450 engineering approaches and highlight the key regions and residues that have been identified using such approaches. These "hotspots" lie within critical functional areas of the P450 structure, including the active site, the substrate access channel, and the redox partner interaction interface.

Indexed as

Crystal structureCytochrome P450Protein engineeringRational design

Identifiers

PMID30533540
PMCPMC6263019
OpenAlexW2897568450

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.