Modular Assembly of Phosphite Dehydrogenase and Phenylacetone Monooxygenase for Tuning Cofactor Regeneration.
Baeyer–Villiger monooxygenase
RIAD–RIDD tag
cofactor regeneration
oligomers
self-assembly
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
17 06 2021
17 06 2021
Historique:
received:
28
05
2021
revised:
10
06
2021
accepted:
13
06
2021
entrez:
2
7
2021
pubmed:
3
7
2021
medline:
23
9
2021
Statut:
epublish
Résumé
The use of multienzyme complexes can facilitate biocatalytic cascade reactions by employing fusion enzymes or protein tags. In this study, we explored the use of recently developed peptide tags that promote complex formation of the targeted proteins: the dimerization-docking and anchoring domain (RIDD-RIAD) system. These peptides allow self-assembly based on specific protein-protein interactions between both peptides and allow tuning of the ratio of the targeted enzymes as the RIAD peptide binds to two RIDD peptides. Each of these tags were added to the C-terminus of a NADPH-dependent Baeyer-Villiger monooxygenase (phenylacetone monooxygenase, PAMO) and a NADPH-regenerating enzyme (phosphite dehydrogenase, PTDH). Several RIDD/RIAD-tagged PAMO and PTDH variants were successfully overproduced in
Identifiants
pubmed: 34204515
pii: biom11060905
doi: 10.3390/biom11060905
pmc: PMC8234031
pii:
doi:
Substances chimiques
Multienzyme Complexes
0
Recombinant Proteins
0
Mixed Function Oxygenases
EC 1.-
NADH, NADPH Oxidoreductases
EC 1.6.-
NAD phosphite oxidoreductase
EC 1.6.99.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
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