Evidence map›Paper›PMID 38466518›Full record

ReviewMolecular biology reports2024

Multidomain chimeric enzymes as a promising alternative for biocatalysts improvement: a minireview.

Flor de María García-Paz, Sandra Del Moral, Sandra Morales-Arrieta, Marcela Ayala, Luis Gerardo Treviño-Quintanilla, Clarita Olvera-Carranza

Open access · hybridAbstract readReview
In one paragraph

Review in Molecular biology reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

6 citing papers in PubMed, 13 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

6 authors at 3 institutions in 1 country.

Flor de María García-PazDepartamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Av. Universidad 2001 Col. Chamilpa CP 62210, Cuernavaca, Morelos, México.ORCID http://orcid.org/0000-0001-6587-6853
Sandra Del MoralInvestigador por México-CONAHCyT, Unidad de Investigación y Desarrollo en Alimentos, Tecnológico Nacional de México, Campus Veracruz. MA de Quevedo 2779, Col. Formando Hogar, CP 91960, Veracruz, Veracruz, México.ORCID http://orcid.org/0000-0001-8815-0465
Sandra Morales-ArrietaDepartamento de Biotecnología, Universidad Politécnica del Estado de Morelos, Boulevard Cuauhnáhuac No. 566 Col. Lomas del Texcal CP 62550, Jiutepec, Morelos, México.
Marcela AyalaDepartamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Av. Universidad 2001 Col. Chamilpa CP 62210, Cuernavaca, Morelos, México.ORCID http://orcid.org/0000-0002-1234-4287
Luis Gerardo Treviño-QuintanillaDepartamento de Biotecnología, Universidad Politécnica del Estado de Morelos, Boulevard Cuauhnáhuac No. 566 Col. Lomas del Texcal CP 62550, Jiutepec, Morelos, México.ORCID http://orcid.org/0000-0002-6677-9630
Clarita Olvera-CarranzaDepartamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Av. Universidad 2001 Col. Chamilpa CP 62210, Cuernavaca, Morelos, México. clarita.olvera@ibt.unam.mx.ORCID http://orcid.org/0000-0002-8364-5845
Universidad Autónoma del Estado de Morelos · MXUniversidad Politecnica del Estado de Morelos · MXInstituto Tecnologico de Veracruz · MX

Funding

Consejo Nacional de Ciencia y Tecnología 21620, 154383 and 183795Universidad Nacional Autónoma de México-Programa de Apoyo a Proyectos de Investigación e Innovación Tecnológica IN227723
6 · The paper itself

Abstract

Searching for new and better biocatalysts is an area of study in constant development. In nature, mechanisms generally occurring in evolution, such as genetic duplication, recombination, and natural selection processes, produce various enzymes with different architectures and properties. The recombination of genes that code proteins produces multidomain chimeric enzymes that contain two or more domains that sometimes enhance their catalytic properties. Protein engineering has mimicked this process to enhance catalytic activity and the global stability of enzymes, searching for new and better biocatalysts. Here, we present and discuss examples from both natural and synthetic multidomain chimeric enzymes and how additional domains heighten their stability and catalytic activity. Moreover, we also describe progress in developing new biocatalysts using synthetic fusion enzymes and revise some methodological strategies to improve their biological fitness.

Indexed as

Gene DuplicationProtein EngineeringBiocatalysisCatalysisEnzymesRecombinant Fusion ProteinsEnzymesRecombinant Fusion ProteinsChimeric enzymesEnzyme activityEnzyme stabilityFusion enzymesMultidomain enzymes

Identifiers

PMID38466518
PMCPMC10927867
OpenAlexW4392659906

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.