Chimeric versus isolated proteins: Biochemical characterization of the NADP
Fused enzymes
Protein conformation
Protein promiscuity
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
31 Dec 2023
31 Dec 2023
Historique:
received:
16
05
2023
revised:
04
08
2023
accepted:
29
08
2023
medline:
27
11
2023
pubmed:
2
9
2023
entrez:
1
9
2023
Statut:
ppublish
Résumé
The expression of multifunctional proteins can facilitate the setup of a biotechnology process that requires multiple functions absolved by different proteins. Herein the functional and conformational characterization of a formate dehydrogenase-monooxygenase chimera enzyme is presented. The fused enzyme (FDH-PAMO) was prepared by linking the C-terminus of the mutant NADP
Identifiants
pubmed: 37657580
pii: S0141-8130(23)03533-X
doi: 10.1016/j.ijbiomac.2023.126637
pii:
doi:
Substances chimiques
Mixed Function Oxygenases
EC 1.-
NADP
53-59-8
Formate Dehydrogenases
EC 1.17.1.9
NADPH Dehydrogenase
EC 1.6.99.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
126637Informations de copyright
Copyright © 2023 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Francesco Secundo reports financial support was provided by European Union. Anastasia A. Pometun reports financial support was provided by Russian Foundation for Basic Research and Moscow Government. S. Yu Kleymenov reports financial support was provided by Ministry of Science and Higher Education of Russia.