# Multidisciplinary approaches for enzyme biocatalysis in pharmaceuticals: protein engineering, computational biology, and nanoarchitectonics

https://mdr.nims.go.jp/datasets/8431ae16-1068-4452-8ad7-2b47d4eb65d7

## Files

- [EESCatal24_2_14.pdf](https://mdr.nims.go.jp/filesets/19ae1a07-c631-496d-a988-d75d2b1f5768/download) ([Detail](https://mdr.nims.go.jp/filesets/19ae1a07-c631-496d-a988-d75d2b1f5768.md))

## Id

8431ae16-1068-4452-8ad7-2b47d4eb65d7

## Local identifier



## Visibility

open_to_public

## State

published

## Created at

2024-01-13T00:20:51.329135Z

## Updated at

2024-01-18T07:57:46.919326Z

## Published at

2024-01-18T23:30:14.407513Z

## Doi



## First published url

https://doi.org/10.1039/d3ey00239j

## Date published

2023-10-28

## Recorded date published

2024-1-11

## Resource type

journal_article

## Manuscript type

vor

## Collection



## Title

- title: 'Multidisciplinary approaches for enzyme biocatalysis in pharmaceuticals:
    protein engineering, computational biology, and nanoarchitectonics'
  title_type: original
  lang: en

## Description

- description: Enzyme biocatalysis is reshaping pharmaceutical synthesis, offering
    sustainable and efficient pathways for drug discovery and production. This paradigm
    shift towards eco-friendly methodologies addresses concerns inherent in traditional
    chemical synthesis. Enzymes, celebrated for their precision and adaptability to
    mild conditions, are poised as ideal candidates for pharmaceutical applications.
    Their versatility facilitates the synthesis of diverse pharmaceutical compounds,
    ensuring precise drug design and minimizing environmental impact. The integration
    of multidisciplinary approaches, including protein engineering, computational
    biology, and nanoarchitectonics, holds the potential to propel enzyme biocatalysis
    even further. Protein engineering utilizes directed evolution and rational design
    to customize enzymes, enhancing their stability and efficacy.
  description_type: abstract
  lang: eng

## Creator

- name: Suhyeon Kim
  role: author
  orcid: https://orcid.org/0000-0001-8375-2491
- name: Seongmin Ga
  role: author
  orcid: https://orcid.org/0009-0004-9200-1189
- name: Hayeon Bae
  role: author
  orcid: https://orcid.org/0009-0001-1138-4615
- name: Ronald Sluyter
  role: author
  orcid: https://orcid.org/0000-0003-4909-686X
- name: Konstantin Konstantinov
  role: author
  orcid: https://orcid.org/0000-0003-4919-6385
- name: Lok Kumar Shrestha
  role: author
  orcid: https://orcid.org/0000-0003-2680-6291
  organization: National Institute for Materials Science
- name: Yong Ho Kim
  role: author
  orcid: https://orcid.org/0000-0002-9106-3298
- name: Jung Ho Kim
  role: author
  orcid: https://orcid.org/0000-0003-4931-3553
- name: Katsuhiko Ariga
  role: author
  orcid: https://orcid.org/0000-0002-2445-2955
  organization: National Institute for Materials Science

## Contact agent



## Publisher

organization: Royal Society of Chemistry (RSC)

## Managing organization



## Keyword

- subject: enzyme
  schema: not_defined
- subject: biocatalysis
  schema: not_defined
- subject: protein
  schema: not_defined

## Rights

- identifier: https://creativecommons.org/licenses/by-nc/3.0/legalcode

## Other identifier(s)



## Data origin

- data_origin_type: other

## Embargo



## Journal

- title: EES Catalysis
  issn: 2753801X
  volume: '2'
  issue: '1'
  start_page: 14
  end_page: 48

## Conference



## Related item



## Funding

- identifier: 023R1A2C3005731
  funder_name: National Research Foundation of Korea
- identifier: 2021R1A4A1033424
  funder_name: National Research Foundation of Korea

## Instrument



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## Measurement method



## Specimen



## Chemical composition



## Structure for specimen



## Structural feature for specimen



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## Computational method



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## Fileset

- id: 19ae1a07-c631-496d-a988-d75d2b1f5768
  filename: EESCatal24_2_14.pdf
  content_type: application/pdf
  size: 8930519
  md5: 145010393dffa40abcf50f2fe18f8c67

## Thumbnail

fileset_id: 19ae1a07-c631-496d-a988-d75d2b1f5768
filename: EESCatal24_2_14.pdf