Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 67, 2003 - Issue 9
Journal homepage
380
Views
69
CrossRef citations to date
0
Altmetric
Original Articles

Fosmidomycin Resistance in Adenylate Cyclase Deficient (cya) Mutants of Escherichia coli

Yoshiko SAKAMOTODepartment of Food Science and Technology, College of Bioresouce Sciences, Nihon UniversityKameino 1866, Fujisawa, Kanagawa 252-8510, Japan
,
Soichi FURUKAWADepartment of Food Science and Technology, College of Bioresouce Sciences, Nihon UniversityKameino 1866, Fujisawa, Kanagawa 252-8510, Japan
,
Hirokazu OGIHARADepartment of Food Science and Technology, College of Bioresouce Sciences, Nihon UniversityKameino 1866, Fujisawa, Kanagawa 252-8510, Japan
&
Makari YAMASAKIDepartment of Food Science and Technology, College of Bioresouce Sciences, Nihon UniversityKameino 1866, Fujisawa, Kanagawa 252-8510, Japan
Pages 2030-2033 | Received 10 Apr 2003, Accepted 16 Jun 2003, Published online: 22 May 2014
 
Sample our Environment & Agriculture journals, sign in here to start your access, latest two full volumes FREE to you for 14 days

Abstract

Adenylate cyclase deficient (cya) mutants of E. coli K-12 were found to be resistant to fosmidomycin, a specific inhibitor of the non-mevalonate pathway, just like to fosfomycin. E. coli glpT mutants were resistant to fosfomycin and also to fosmidomycin. This fact shows that fosmidomycin was transported inside via the glycerol-3-phosphate transporter, GlpT. DNA micro-array analysis showed that the transcription of glpT and other genes concerning glycerol utilization were highly dependent on the presence of cAMP.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related Research Data

Isolation of Genomic Deoxyxylulose Phosphate Reductoisomerase (DXR) Mutations Conferring Resistance to Fosmidomycin
Source: Cold Spring Harbor Laboratory
Fosfomycin: evaluation of the published evidence on the emergence of antimicrobial resistance in Gram-negative pathogens
Source: Oxford University Press (OUP)
Identification of potential drug targets and inhibitor of the pathogenic bacteria Shigella flexneri 2a through the subtractive genomic approach
Source: Springer Science and Business Media LLC
The intriguing biology and chemistry of fosfomycin: the only marketed phosphonate antibiotic
Source: Royal Society of Chemistry (RSC)
Growth medium-dependent antimicrobial activity of early stage MEP pathway inhibitors.
Source: Public Library of Science (PLoS)
Resistance to the Antimicrobial Agent Fosmidomycin and an FR900098 Prodrug through Mutations in the Deoxyxylulose Phosphate Reductoisomerase Gene (dxr)
Source: American Society for Microbiology
The Bacterial Cell Wall as a Target for Antibiotics
Source: Wiley
Potent, specific MEPicides for treatment of zoonotic staphylococci
Source: Cold Spring Harbor Laboratory
Fosmidomycin Uptake into Plasmodium and Babesia-Infected Erythrocytes Is Facilitated by Parasite-Induced New Permeability Pathways
Source: Public Library of Science (PLoS)
Apicoplast isoprenoid precursor synthesis and the molecular basis of fosmidomycin resistance in Toxoplasma gondii
Source: Rockefeller University Press

Linking provided by 
Download PDF

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.