Evidence map›Paper›PMID 31811088›Full record

ReviewThe Journal of biological chemistry2020

Engineering cytochrome P450 enzyme systems for biomedical and biotechnological applications.

Zhong Li, Yuanyuan Jiang, F Peter Guengerich, Li Ma, Shengying Li, Wei Zhang

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
18.8field-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

108 citing papers in PubMed, 153 citations in OpenAlex.

  1. Article
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  8. Review
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  14. A novel P450 enzyme assay utilizing an NADPBiotechnology letters · 2025
    Article
  15. Article
  16. Article
  17. An Update: Enzymatic Synthesis for Industrial Applications.Angewandte Chemie (International ed. in English) · 2025
    Review
  18. Article
  19. Review
  20. Article

48 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

6 authors at 2 institutions in 2 countries.

Zhong LiShandong Provincial Key Laboratory of Synthetic Biology and CAS Key Laboratory of Biofuels at Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, Shandong 266101, China.
Yuanyuan JiangShandong Provincial Key Laboratory of Synthetic Biology and CAS Key Laboratory of Biofuels at Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, Shandong 266101, China.
F Peter GuengerichDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146.ORCID 0000-0002-7458-3048
Li MaState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong 266237, China.
Shengying LiState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong 266237, China.
Wei ZhangState Key Laboratory of Microbial Technology, Shandong University, Qingdao, Shandong 266237, China zhang_wei@sdu.edu.cn.ORCID 0000-0001-9459-680X
Shandong University · CNVanderbilt University · US

Funding

Metabolism of Carcinogens and Drugs by Human P450sR01GM118122 · NIGMS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 2016 to 2023
$3.3M
NIGMS NIH HHS R01 GM118122
6 · The paper itself

Abstract

Cytochrome P450 enzymes (P450s) are broadly distributed among living organisms and play crucial roles in natural product biosynthesis, degradation of xenobiotics, steroid biosynthesis, and drug metabolism. P450s are considered as the most versatile biocatalysts in nature because of the vast variety of substrate structures and the types of reactions they catalyze. In particular, P450s can catalyze regio- and stereoselective oxidations of nonactivated C-H bonds in complex organic molecules under mild conditions, making P450s useful biocatalysts in the production of commodity pharmaceuticals, fine or bulk chemicals, bioremediation agents, flavors, and fragrances. Major efforts have been made in engineering improved P450 systems that overcome the inherent limitations of the native enzymes. In this review, we focus on recent progress of different strategies, including protein engineering, redox-partner engineering, substrate engineering, electron source engineering, and P450-mediated metabolic engineering, in efforts to more efficiently produce pharmaceuticals and other chemicals. We also discuss future opportunities for engineering and applications of the P450 systems.

Indexed as

BiotechnologyBiocatalysisCytochrome P-450 Enzyme SystemMetabolic EngineeringProtein EngineeringSteroidsSubstrate SpecificityXenobioticsCytochrome P-450 Enzyme SystemSteroidsXenobioticscytochrome P450directed evolutionelectron source engineeringenzyme mechanismferredoxinlight activationmetabolic engineeringprotein engineeringredox partner proteinssubstrate engineeringsubstrate specificity

Identifiers

PMID31811088
PMCPMC6970918
OpenAlexW2993040703

What OpenQuestion holds

Textmetadata
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.