Identification, functional and structural characterization of novel aminoglycoside phosphotransferase APH(3″)-Id from Streptomyces rimosus subsp. rimosus ATCC 10970.
Amino Acid Sequence
Anti-Bacterial Agents
/ pharmacology
Bacterial Proteins
/ chemistry
Computational Biology
Escherichia coli
/ drug effects
Genes, Bacterial
Phosphorylation
Phosphotransferases (Alcohol Group Acceptor)
/ chemistry
Phylogeny
Protein Processing, Post-Translational
Protein Structure, Tertiary
Recombinant Proteins
/ chemistry
Sequence Alignment
Streptomyces rimosus
/ enzymology
Streptomycin
/ pharmacology
3D structure
APH(3″)-Id
Aminoglycoside phosphotransferase
Antibiotic resistance
Streptomyces rimosus
Streptomycin phosphotransferase
X-ray
Journal
Archives of biochemistry and biophysics
ISSN: 1096-0384
Titre abrégé: Arch Biochem Biophys
Pays: United States
ID NLM: 0372430
Informations de publication
Date de publication:
15 08 2019
15 08 2019
Historique:
received:
21
01
2019
revised:
21
06
2019
accepted:
22
06
2019
pubmed:
30
6
2019
medline:
17
3
2020
entrez:
29
6
2019
Statut:
ppublish
Résumé
In this study, we identified a new gene (aph(3″)-Id) coding for a streptomycin phosphotransferase by using phylogenetic comparative analysis of the genome of the oxytetracycline-producing strain Streptomyces rimosus ATCC 10970. Cloning the aph(3″)-Id gene in E.coli and inducing its expression led to an increase in the minimum inhibitory concentration of the recombinant E.coli strain to streptomycin reaching 350 μg/ml. To evaluate the phosphotransferase activity of the recombinant protein APH(3″)-Id we carried out thin-layer chromatography of the putative
Identifiants
pubmed: 31251922
pii: S0003-9861(19)30045-1
doi: 10.1016/j.abb.2019.06.008
pii:
doi:
Substances chimiques
Anti-Bacterial Agents
0
Bacterial Proteins
0
Recombinant Proteins
0
Phosphotransferases (Alcohol Group Acceptor)
EC 2.7.1.-
streptomycin 3''-kinase
EC 2.7.1.87
Streptomycin
Y45QSO73OB
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
111-122Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.