Evidence map›Paper›PMID 39191403›Full record

ArticlemBio2024

Rational design of a flavoenzyme for aerobic nicotine catabolism.

Haiyang Hu, Zhaoyong Xu, Zhiyao Zhang, Peizhi Song, Frederick Stull, Ping Xu, Hongzhi Tang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mBio, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Haiyang Hu *State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic and Developmental Sciences, and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.ORCID 0000-0002-2059-5115
Zhaoyong Xu *State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic and Developmental Sciences, and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Zhiyao ZhangDepartment of Chemistry, Western Michigan University, Kalamazoo, Michigan, USA.
Peizhi SongState Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic and Developmental Sciences, and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Frederick StullDepartment of Chemistry, Western Michigan University, Kalamazoo, Michigan, USA.
Ping XuState Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic and Developmental Sciences, and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Hongzhi TangState Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic and Developmental Sciences, and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.ORCID 0000-0002-7743-0186

Funding

Mechanistic basis for the low O2-dependent activity of a nicotine-degrading enzymeR15GM139069 · NIGMS · WESTERN MICHIGAN UNIVERSITY · PI STULL, FREDERICK · 2021 to 2021
$449k
HHS | National Institutes of Health (NIH) R15GM139069MOST | National Key Research and Development Program of China (NKPs) 2021YFA0909500MOST | National Natural Science Foundation of China (NSFC) 32030004NIGMS NIH HHS R15 GM139069the Oceanic Interdisciplinary Program of Shanghai Jiao Tong University SL2020MS027
6 · The paper itself

Abstract

Enzymatic therapy with nicotine-degrading enzyme is a new strategy in treating nicotine addiction, which can reduce nicotine concentrations and weaken withdrawal in the rat model. However, when O IMPORTANCE: Nicotine, the main active substance in tobacco, results in cigarette addiction and various diseases. There have been some attempts at using nicotine oxidoreductase, NicA2, as a therapeutic for nicotine cessation. However, it uses cytochrome c as it is electron acceptor, which is impractical for therapeutic use compared with using O2 as an oxidant. Thus, amino acid alteration was performed on Pnao using NicA2 as model. Five of the mutants generated degraded nicotine at a rate similar to NicA2, and one of the catabolic compounds was identified as nicotine-1'-N-oxide. Our research highlights a new direction in developing enzymes that efficiently catabolize nicotine without co-enzymes and suggests that structure-similar human original MAOA (or B) may assist with nicotine cessation after being engineered.

Indexed as

NicotineAerobiosisAnimalsOxygenProtein EngineeringRatsNicotineOxygenenzyme engineeringnicotine catabolismrational design

Identifiers

PMID39191403
PMCPMC11481913

What OpenQuestion holds

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LicenceCC BY
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.