Evidence map›Paper›PMID 27253324›Full record

ArticlePloS one2016

Modeling and Re-Engineering of Azotobacter vinelandii Alginate Lyase to Enhance Its Catalytic Efficiency for Accelerating Biofilm Degradation.

Chul Ho Jang, Yu Lan Piao, Xiaoqin Huang, Eun Jeong Yoon, So Hee Park, Kyoung Lee, Chang-Guo Zhan, Hoon Cho

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 41 citations in OpenAlex.

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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

8 authors at 4 institutions in 2 countries.

Chul Ho JangDepartment of Otolaryngology, Chonnam National University Medical School, Gwangju, 501-757, Republic of Korea.
Yu Lan PiaoDepartment of Polymer Science & Engineering, Chosun University, Gwangju, 501-759, South Korea.
Xiaoqin HuangMolecular Modeling and Biopharmaceutical Center and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, Kentucky, 40536, United States of America.
Eun Jeong YoonDepartment of Polymer Science & Engineering, Chosun University, Gwangju, 501-759, South Korea.
So Hee ParkDepartment of Polymer Science & Engineering, Chosun University, Gwangju, 501-759, South Korea.
Kyoung LeeDepartment of Microbiology, Changwon National University, Changwon, Kyongnam, 641-773, Republic of Korea.
Chang-Guo ZhanMolecular Modeling and Biopharmaceutical Center and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, Kentucky, 40536, United States of America.
Hoon ChoDepartment of Polymer Science & Engineering, Chosun University, Gwangju, 501-759, South Korea.
Chosun University · KRUniversity of Kentucky · USChangwon National University · KRChonnam National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alginate is known to prevent elimination of Pseudomonas aeruginosa biofilms. Alginate lyase (AlgL) might therefore facilitate treatment of Pseudomonas aeruginosa-infected cystic fibrosis patients. However, the catalytic activity of wild-type AlgL is not sufficiently high. Therefore, molecular modeling and site-directed mutagenesis of AlgL might assist in enzyme engineering for therapeutic development. AlgL, isolated from Azotobacter vinelandii, catalyzes depolymerization of alginate via a β-elimination reaction. AlgL was modeled based on the crystal structure template of Sphingomonas AlgL species A1-III. Based on this computational analysis, AlgL was subjected to site-directed mutagenesis to improve its catalytic activity. The kcat/Km of the K194E mutant showed a nearly 5-fold increase against the acetylated alginate substrate, as compared to the wild-type. Double and triple mutants (K194E/K245D, K245D/K319A, K194E/K245D/E312D, and K194E/K245D/K319A) were also prepared. The most potent mutant was observed to be K194E/K245D/K319A, which has a 10-fold improved kcat value (against acetylated alginate) compared to the wild-type enzyme. The antibiofilm effect of both AlgL forms was identified in combination with piperacillin/tazobactam (PT) and the disruption effect was significantly higher in mutant AlgL combined with PT than wild-type AlgL. However, for both the wild-type and K194E/K245D/K319A mutant, the use of the AlgL enzyme alone did not show significant antibiofilm effect.

Indexed as

CatalysisAlginatesAmino Acid SequenceAnti-Bacterial AgentsAzotobacter vinelandiiBiofilmsGlucuronic AcidHexuronic AcidsMutagenesis, Site-DirectedMutant ProteinsPenicillanic AcidPiperacillinPolysaccharide-LyasesPseudomonas aeruginosaTazobactamAlginatesAnti-Bacterial AgentsGlucuronic AcidHexuronic AcidsMutant ProteinsPenicillanic AcidPiperacillinpoly(beta-D-mannuronate) lyasePolysaccharide-LyasesTazobactam

Identifiers

PMID27253324
PMCPMC4890793
OpenAlexW2418185222

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Registered trials

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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.