Promiscuous Esterases Counterintuitively Are Less Flexible than Specific Ones-Reference-Cited by-同舟云学术

Promiscuous Esterases Counterintuitively Are Less Flexible than Specific Ones

Published:2021-05-05 Issue:5 Volume:61 Page:2383-2395
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Nutschel Christina¹,Coscolín Cristina²,David Benoit³,Mulnaes Daniel³,Ferrer Manuel²^ORCID,Jaeger Karl-Erich⁴⁵,Gohlke Holger¹³^ORCID

Affiliation:

1. John von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC), Institute of Biological Information Processing (IBI-7: Structural Biochemistry), and Institute of Bio- and Geosciences (IBG-4: Bioinformatics), Forschungszentrum Jülich GmbH, 52425 Jülich, Germany

2. Institute of Catalysis, Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain

3. Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany

4. Institute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, 52425 Jülich, Germany

5. Institute of Bio- and Geosciences IBG-1: Biotechnology, Forschungszentrum Jülich GmbH, 52425 Jülich, Germany

Funder

Bundesministerium f?r Bildung und Forschung

Ministerio de Ciencia, Innovaci?n y Universidades

European Commission

European Regional Development Fund

Ministerio de Econom?a y Competitividad

Deutsche Forschungsgemeinschaft

Forschungszentrum J?lich

Horizon 2020 Framework Programme

North Rhine Westphalia

Agencia Estatal de Investigaci?n

Agencia Estatal CSIC

Publisher

American Chemical Society (ACS)

Subject

Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.1c00152

Reference73 articles.

1. Shining a light on enzyme promiscuity

2. Molecular insights into the enzyme promiscuity of an aromatic prenyltransferase

3. Panoramic view of a superfamily of phosphatases through substrate profiling

4. Enzyme Promiscuity: A Mechanistic and Evolutionary Perspective

5. Protein promiscuity and its implications for biotechnology

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