Dihydroxy-Acid Dehydratases From Pathogenic Bacteria: Emerging Drug Targets to Combat Antibiotic Resistance.
Fe−S cluster
antibiotics
dihydroxy-acid dehydratase
enzyme activation
sustainable chemistry
Journal
Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783
Informations de publication
Date de publication:
04 Aug 2022
04 Aug 2022
Historique:
received:
25
03
2022
pubmed:
11
5
2022
medline:
9
8
2022
entrez:
10
5
2022
Statut:
ppublish
Résumé
There is an urgent global need for the development of novel therapeutics to combat the rise of various antibiotic-resistant superbugs. Enzymes of the branched-chain amino acid (BCAA) biosynthesis pathway are an attractive target for novel anti-microbial drug development. Dihydroxy-acid dehydratase (DHAD) is the third enzyme in the BCAA biosynthesis pathway. It relies on an Fe-S cluster for catalytic activity and has recently also gained attention as a catalyst in cell-free enzyme cascades. Two types of Fe-S clusters have been identified in DHADs, i.e. [2Fe-2S] and [4Fe-4S], with the latter being more prone to degradation in the presence of oxygen. Here, we characterise two DHADs from bacterial human pathogens, Staphylococcus aureus and Campylobacter jejuni (SaDHAD and CjDHAD). Purified SaDHAD and CjDHAD are virtually inactive, but activity could be reversibly reconstituted in vitro (up to ∼19,000-fold increase with k
Identifiants
pubmed: 35535733
doi: 10.1002/chem.202200927
pmc: PMC9543379
doi:
Substances chimiques
Bacterial Proteins
0
Iron-Sulfur Proteins
0
Hydro-Lyases
EC 4.2.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202200927Subventions
Organisme : Australian Research Council
ID : DP210101802
Organisme : National Health and Medical Research Council, Australia
ID : 2003946
Informations de copyright
© 2022 The Authors. Chemistry - A European Journal published by Wiley-VCH GmbH.
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