Cloning and expression heterologous alanine dehydrogenase genes: Investigation of reductive amination potential of L-alanine dehydrogenases for green synthesis of alanine derivatives.

Active site modelling Green synthesis L-Alanine dehydrogenase Reductive amination mechanism Unnatural amino acids

Journal

Heliyon
ISSN: 2405-8440
Titre abrégé: Heliyon
Pays: England
ID NLM: 101672560

Informations de publication

Date de publication:
15 Mar 2024
Historique:
received: 29 12 2023
revised: 09 02 2024
accepted: 21 02 2024
medline: 11 3 2024
pubmed: 11 3 2024
entrez: 11 3 2024
Statut: epublish

Résumé

Unnatural amino acids (UAAs) offer significant promise in a wide range of applications, including drug discovery, the custom design of peptides and proteins, and their utility and use as markers for monitoring molecular interactions in biological research. The synthesis of UAAs presents a formidable challenge and can be classified into two primary categories: enzymatic and chemical synthesis. Notably, the enzymatic route, specifically asymmetric synthesis, emerges as a an attractive method for procuring enantiopure UAAs with high efficiency, owing to its streamlined and concise reaction mechanism. The current study investigated the reductive amination activity mechanisms of alanine dehydrogenase (L-AlaDH), sourced from a combination of newly and previously characterized microorganisms. Our principal aim was to evaluate the catalytic efficiency of these L-AlaDH enzymes concerning a range of specific ketoacids and pyruvate to ascertain their capability for facilitating the production of both natural and unnatural amino acids. After the characterization processes, mutation points for

Identifiants

pubmed: 38463761
doi: 10.1016/j.heliyon.2024.e26899
pii: S2405-8440(24)02930-X
pmc: PMC10923667
doi:

Types de publication

Journal Article

Langues

eng

Pagination

e26899

Informations de copyright

© 2024 The Authors. Published by Elsevier Ltd.

Déclaration de conflit d'intérêts

The authors declare the following financial interests/personal relationships which may be considered as potential competing interestsBaris Binay reports financial support was provided by The 10.13039/501100004410Scientific and Technological Research Council of Turkey (TUBITAK). Baris Binay reports a relationship with The 10.13039/501100004410Scientific and Technological Research Council of Turkey that includes: funding grants. This work was supported partially by The 10.13039/501100004410Scientific and Technological Research Council of Turkey (TUBITAK) (Project number: 120Z501). If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Ğarip Demir (Ğ)

Department of Molecular Biology and Genetics, Gebze Technical University, 41400, Gebze, Kocaeli, Turkey.

Jarkko Valjakka (J)

Faculty of Medicine and Health Technology, Tampere University, FI-33100, Tampere, Finland.

Ossi Turunen (O)

School of Forest Sciences, University of Eastern Finland, FI-80101, Joensuu, Finland.

Fatih Aktaş (F)

Faculty of Engineering, Düzce University, 81600, Düzce, Turkey.

Barış Binay (B)

Department of Bioengineering, Gebze Technical University, 41400, Gebze, Kocaeli, Turkey.
BAUZYME Biotechnology Co., Gebze Technical University Technopark, 41400, Gebze, Kocaeli, Turkey.

Classifications MeSH