Evidence map›Paper›PMID 39075048›Full record

ArticleNature communications2024

Biocatalysis enables the scalable conversion of biobased furans into various furfurylamines.

Pritam Giri, Seonga Lim, Taresh P Khobragade, Amol D Pagar, Mahesh D Patil, Sharad Sarak, Hyunwoo Jeon, Sangwoo Joo, Younghwan Goh, Seohee Jung and 6 more

Abstract read
In one paragraph

Article in Nature communications, 2024. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Review
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

16 authors.

Pritam GiriDepartment of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.ORCID 0009-0005-8040-5132
Seonga LimDepartment of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.ORCID 0009-0007-3949-3243
Taresh P KhobragadeDepartment of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Amol D PagarDepartment of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Mahesh D PatilChemical Engineering and Process Development Division, CSIR- National Chemical Laboratory, Pune, 411008, India.ORCID 0000-0002-5602-3442
Sharad SarakDepartment of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Hyunwoo JeonDepartment of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Sangwoo JooDepartment of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Younghwan GohDepartment of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Seohee JungDepartment of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Yu-Jeong JangDepartment of Chemistry, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Seung Beom ChoiDepartment of Chemistry, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Ye Chan KimSchool of Chemical and Biological Engineering, Seoul National University, Seoul, Republic of Korea.
Taek Jin KangDepartment of Chemical and Biochemical Engineering, Dongguk University, Seoul, 04620, Republic of Korea.
Yong-Seok HeoDepartment of Chemistry, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea. ysheo@konkuk.ac.kr.ORCID 0000-0003-3080-4109
Hyungdon YunDepartment of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea. hyungdon@konkuk.ac.kr.ORCID 0000-0002-9125-975X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biobased furans have emerged as chemical building blocks for the development of materials because of their diverse scaffolds and as they can be directly prepared from sugars. However, selective, efficient, and cost-effective scalable conversion of biobased furans remains elusive. Here, we report a robust transaminase (TA) from Shimia marina (SMTA) that enables the scalable amination of biobased furanaldehydes with high activity and broad substrate specificity. Crystallographic and mutagenesis analyses provide mechanistic insights and a structural basis for understanding SMTA, which enables a higher substrate conversion. The enzymatic cascade process established in this study allows one-pot synthesis of 2,5-bis(aminomethyl)furan (BAMF) and 5-(aminomethyl)furan-2-carboxylic acid from 5-hydroxymethylfurfural. The biosynthesis of various furfurylamines, including a one-pot cascade reaction for BAMF generation using whole cells, demonstrates their practical application in the pharmaceutical and polymer industries.

Indexed as

BiocatalysisFuransTransaminasesAminationAminesCrystallography, X-RayFuraldehydeSubstrate Specificity5-hydroxymethylfurfuralAminesFuraldehydeFuransTransaminases

Identifiers

PMID39075048
PMCPMC11286754

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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.