Expression, Purification, and Biophysical Characterization of Klebsiella Pneumoniae Nicotinate Nucleotide Adenylyltransferase.
Dual enzyme assay
Isothermal titration calorimetry
Klebsiella pneumoniae
Nicotinate nucleotide adenylyltransferase
Recombinant expression
Journal
The protein journal
ISSN: 1875-8355
Titre abrégé: Protein J
Pays: Netherlands
ID NLM: 101212092
Informations de publication
Date de publication:
02 2022
02 2022
Historique:
accepted:
20
12
2021
pubmed:
28
1
2022
medline:
22
3
2022
entrez:
27
1
2022
Statut:
ppublish
Résumé
Patients in health-care settings develop nosocomial infections due to prolonged hospital stay. The Gram negative Klebsiella pneumoniae (K. pneumoniae), is a bacterial pathogen responsible for most nosocomial infections and are resistant to most current antibiotics. Hence, there is need for identification and validation of potential protein targets for design of new generation antibiotics. One of such targets is nicotinate nucleotide adenylyltransferase, an enzyme responsible for redox metabolism. This study focuses on novel expression, purification, and biophysical characterization of NNAT from K. pneumoniae. KpNNAT was over-expressed in T7 express™ Escherichia coli using the pGEX-4 T-1 expressions system and purified to > 98% homogeneity (~ 20 mg KpNNAT/g of the wet cell) using a combination of glutathione-agarose and immobilized Ni
Identifiants
pubmed: 35083643
doi: 10.1007/s10930-021-10037-2
pii: 10.1007/s10930-021-10037-2
doi:
Substances chimiques
Nicotinamide-Nucleotide Adenylyltransferase
EC 2.7.7.1
nicotinic acid mononucleotide adenylyltransferase
EC 2.7.7.18
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
141-156Informations de copyright
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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