Evidence map›Paper›PMID 31652673›Full record

ArticleInternational journal of molecular sciences2019

Disulfide Engineered Lipase to Enhance the Catalytic Activity: A Structure-Based Approach on BTL2.

César A Godoy, Javier Klett, Bruno Di Geronimo, Juan A Hermoso, José M Guisán, César Carrasco-López

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

9 citing papers in PubMed, 23 citations in OpenAlex.

  1. Recent insight into the advances and prospects of microbial lipases and their potential applications in industry.International microbiology : the official journal of the Spanish Society for Microbiology · 2024
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Insertion of a synthetic switch into insulin provides metabolite-dependent regulation of hormone-receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Single Residue Substitution atMolecules (Basel, Switzerland) · 2020
    Article
  9. Functional Heterologous Expression of Mature Lipase LipA fromInternational journal of molecular sciences · 2020
    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 5 institutions in 3 countries.

César A GodoyDepartamento de Química (LIBB), Grupo de Investigación en Ingeniería de los Procesos Agroalimentarios y Biotecnológicos (GIPAB), Universidad del Valle, C.P. 76001 Cali, Colombia. cesar.godoy@correounivalle.edu.co.ORCID 0000-0003-4393-9889
Javier KlettExperimental Therapeutics Programme, Spanish National Cancer Research Centre (CNIO), C/Melchor Fernández Almagro 3, E-28029 Madrid, Spain. jklett@cnio.es.ORCID 0000-0001-8495-6568
Bruno Di GeronimoExperimental Therapeutics Programme, Spanish National Cancer Research Centre (CNIO), C/Melchor Fernández Almagro 3, E-28029 Madrid, Spain. bdigeronimo@ext.cnio.es.
Juan A HermosoDepartment of Crystallography and Structural Biology, Institute of Physical Chemistry "Rocasolano" (IQFR-CSIC), E_28006 Madrid, Spain. xjuan@iqfr.csic.es.
José M GuisánDepartamento de Biocatálisis. Instituto de Catálisis. CSIC. Campus UAM. Cantoblanco. C.P. 28049 Madrid, Spain. jmguisan@icp.csic.es.ORCID 0000-0003-1627-6522
César Carrasco-LópezDepartment of Chemical and Biological Engineering, Hoyt Laboratory, Princeton University, Princeton, NJ 08544, USA. cesarc@princeton.edu.
Spanish National Cancer Research Centre · ESInstituto de Catálisis y Petroleoquímica · ESInstituto de Química Física Blas Cabrera · ESPrinceton University · USUniversidad del Valle · CO

Funding

Departamento Administrativo de Ciencia, Tecnología e Innovación 745-2016-Project 110671250425Ministerio de Ciencia y Tecnología BIO-2005-6018576, BFU2017-90030-P and BFU2011-25326Ministerio de Economía, Industria y Competitividad, Gobierno de España FPUUniversidad del Valle CI 71083
6 · The paper itself

Abstract

Enhancement, control, and tuning of hydrolytic activity and specificity of lipases are major goals for the industry. Thermoalkaliphilic lipases from the I.5 family, with their native advantages such as high thermostability and tolerance to alkaline pHs, are a target for biotechnological applications. Although several strategies have been applied to increase lipases activity, the enhancement through protein engineering without compromising other capabilities is still elusive. Lipases from the I.5 family suffer a unique and delicate double lid restructuration to transition from a closed and inactive state to their open and enzymatically active conformation. In order to increase the activity of the wild type

Indexed as

Catalytic DomainAmino Acid SubstitutionBacterial ProteinsCysteineDisulfidesEnzymes, ImmobilizedEnzyme StabilityGeobacillusLipaseMolecular Dynamics SimulationBacterial ProteinsCysteineDisulfidesEnzymes, ImmobilizedLipaseengineered disulfide bondengineered lipaseinterfacial activationlipases activity enhancementthermoalkaliphilic lipase

Identifiers

PMID31652673
PMCPMC6862113
OpenAlexW2982272364

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.