Evidence map›Paper›PMID 35628632›Full record

ArticleInternational journal of molecular sciences2022

Structural Basis for the Regiospecificity of a Lipase from

Zexin Zhao, Siyue Chen, Long Xu, Jun Cai, Jia Wang, Yonghua Wang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

3 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. A Novel Lipase fromInternational journal of molecular sciences · 2023
    Article
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 4 institutions in 1 country.

Zexin ZhaoKey Laboratory of Fermentation Engineering (Ministry of Education), Hubei Key Laboratory of Industrial Microbiology, Hubei University of Technology, Wuhan 430068, China.ORCID 0000-0001-8975-7664
Siyue ChenSchool of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
Long XuCollege of Food Science and Technology, Henan Agricultural University, Zhengzhou 450002, China.
Jun CaiKey Laboratory of Fermentation Engineering (Ministry of Education), Hubei Key Laboratory of Industrial Microbiology, Hubei University of Technology, Wuhan 430068, China.
Jia WangCollege of Life Science, Guangzhou University, Guangzhou 510006, China.
Yonghua WangSchool of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
Hubei University of Technology · CNSouth China University of Technology · CNGuangzhou University · CNHenan Agricultural University · CN

Funding

Key Program of National Natural Science Foundation of China 31930084National Natural Science Foundation of China 31801462National Natural Science Foundation of China 32001639National Science Fund for Distinguished Young Scholars of China 31725022Open Project Funding of the Key Laboratory of Fermentation Engineering(Ministry of Education) 202105FE07Research Fund for the Doctoral Program of Hubei University of Technology BSQD2020036
6 · The paper itself

Abstract

The efficiency and accuracy of the synthesis of structural lipids are closely related to the regiospecificity of lipases. Understanding the structural mechanism of their regiospecificity contributes to the regiospecific redesign of lipases for meeting the technological innovation needs. Here, we used a thermostable lipase from Streptomyces sp. W007 (MAS1), which has been recently reported to show great potential in industry, to gain an insight into the structural basis of its regiospecificity by molecular modelling and mutagenesis experiments. The results indicated that increasing the steric hindrance of the site for binding a non-reactive carbonyl group of TAGs could transform the non-specific MAS1 to a α-specific lipase, such as the mutants G40E, G40F, G40Q, G40R, G40W, G40Y, N45Y, H108W and T237Y (PSI > 80). In addition, altering the local polarity of the site as well as the conformational stability of its composing residues could also impact the regiospecificity. Our present study could not only aid the rational design of the regiospecificity of lipases, but open avenues of exploration for further industrial applications of lipases.

Indexed as

StreptomycesLipaseModels, MolecularLipaselipasemutagenesis studyprotein engineeringstructure-function relationshipsubstrate-binding pocket

Identifiers

PMID35628632
PMCPMC9146090
OpenAlexW4281285389

What OpenQuestion holds

Textmetadata
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.