Structural and Functional Insight into the Mechanism of the Fe-S Cluster-Dependent Dehydratase from Paralcaligenes ureilyticus.
Fe−S cluster
biomanufacturing
branched-chain amino acid biosynthesis
cell-free enzyme cascades
dehydratase
isobutanol
Journal
Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783
Informations de publication
Date de publication:
10 Feb 2023
10 Feb 2023
Historique:
received:
10
10
2022
pubmed:
18
11
2022
medline:
14
2
2023
entrez:
17
11
2022
Statut:
ppublish
Résumé
Enzyme-catalyzed reaction cascades play an increasingly important role for the sustainable manufacture of diverse chemicals from renewable feedstocks. For instance, dehydratases from the ilvD/EDD superfamily have been embedded into a cascade to convert glucose via pyruvate to isobutanol, a platform chemical for the production of aviation fuels and other valuable materials. These dehydratases depend on the presence of both a Fe-S cluster and a divalent metal ion for their function. However, they also represent the rate-limiting step in the cascade. Here, catalytic parameters and the crystal structure of the dehydratase from Paralcaligenes ureilyticus (PuDHT, both in presence of Mg
Identifiants
pubmed: 36385513
doi: 10.1002/chem.202203140
pmc: PMC10107998
doi:
Substances chimiques
Hydro-Lyases
EC 4.2.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202203140Subventions
Organisme : Australian Research Council
ID : DP210101802
Organisme : National Health and Medical Research Centre (AU)
ID : 2003946)
Informations de copyright
© 2022 The Authors. Chemistry - A European Journal published by Wiley-VCH GmbH.
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