Evidence map›Paper›PMID 29440726›Full record

ArticleScientific reports2018

A chemoenzymatic process for amide bond formation by an adenylating enzyme-mediated mechanism.

Ryotaro Hara, Kengo Hirai, Shin Suzuki, Kuniki Kino

Abstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Enzymatic Late-Stage Modifications: Better Late Than Never.Angewandte Chemie (International ed. in English) · 2021
    Review
  7. Enzymkatalysierte späte Modifizierungen: Besser spät als nie.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Review
  8. Article
  9. The Biosynthesis and Metabolism of theFrontiers in molecular biosciences · 2021
    Review
  10. Article
  11. Diamine Biosynthesis: Research Progress and Application Prospects.Applied and environmental microbiology · 2020
    Review
  12. Article
  13. Article
  14. 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

4 authors.

Ryotaro HaraResearch Institute for Science and Engineering, Waseda University, Tokyo, 169-8555, Japan.
Kengo HiraiDepartment of Applied Chemistry, Faculty of Science and Engineering, Waseda University, Tokyo, 169-8555, Japan.
Shin SuzukiDepartment of Applied Chemistry, Faculty of Science and Engineering, Waseda University, Tokyo, 169-8555, Japan.
Kuniki KinoResearch Institute for Science and Engineering, Waseda University, Tokyo, 169-8555, Japan. kkino@waseda.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amide bond formation serves as a fundamental reaction in chemistry, and is practically useful for the synthesis of peptides, food additives, and polymers. However, current methods for amide bond formation essentially generate wastes and suffer from poor atom economy under harsh conditions. To solve these issues, we demonstrated an alternative synthesis method for diverse tryptophyl-N-alkylamides by the combination of the first adenylation domain of tyrocidine synthetase 1 with primary or secondary amines as nucleophiles. Moreover, the physiological role of this domain is L-phenylalanine adenylation; however, we revealed that it displayed broad substrate flexibility from mono-substituted tryptophan analogues to even D-tryptophan. To the best of our knowledge, this is the first evidence for an adenylating enzyme-mediated direct amide bond formation via a sequential enzymatic activation of amino acids followed by nucleophilic substitution by general amines. These findings facilitate the design of a promising tool for biocatalytic straightforward amide bond formation with less side products.

Indexed as

Adenosine MonophosphateAmidesPeptide SynthasesPhenylalanineSubstrate SpecificityAdenosine MonophosphateAmidesPeptide SynthasesPhenylalaninetyrocidine synthetase

Identifiers

PMID29440726
PMCPMC5811625

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Registered trials

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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.