Difference between revisions of "PMID:6352681"

From omp dev
Jump to: navigation, search
(New PMID: Page!)
 
(Fill PMID: Page!)
 
Line 1: Line 1:
 +
{{RightTOC}}
  
 +
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.2871.H4f58f6765de10-->
 +
<!--
 +
******************************************************************************************
 +
*
 +
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
 +
*
 +
****************************************************************************************** -->
 +
{|  id="H4f58f6765de10"  class=" tableEdit PMID_info_table" 
 +
 +
|-
 +
!align=left  |Citation
 +
||
 +
'''Braun, V, Günthner, K, Hantke, K and Zimmermann, L'''  (1983) Intracellular activation of albomycin in Escherichia coli and Salmonella typhimurium.''J. Bacteriol.'' '''156''':308-15
 +
|-
 +
!align=left  |Abstract
 +
||
 +
The antibiotic albomycin is actively taken up by Escherichia coli via the transport system for the structurally similar iron complex ferrichrome. Albomycin is cleaved, and the antibiotically active moiety is released into the cytoplasm, whereas the iron carrier moiety appears in the medium. Besides transport-negative mutants, additional albomycin-resistant mutants were isolated. The mutations were mapped outside the transport genes close to the pyrD gene at 21 min. The mutants were devoid of peptidase N activity. The molecular weight, sensitivity to inhibitors, and cytoplasmic location of the enzyme hydrolyzing albomycin in vitro corresponded to the known properties of peptidase N. The aminoacyl thioribosyl pyrimidine moiety of albomycin apparently has to be cleaved off the iron chelate transport vehicle to inhibit growth. Peptidase N is the major hydrolyzing enzyme. In Salmonella typhimurium peptidase N and peptidase A were equally active in hydrolyzing and activating albomycin.
 +
|-
 +
!align=left  |Links
 +
||
 +
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6352681 PubMed]
 +
 +
|-
 +
!align=left  |Keywords
 +
||
 +
Aminopeptidases; Anti-Bacterial Agents; Aspartic Acid Endopeptidases; Biotransformation; Endopeptidases; Escherichia coli; Ferrichrome; Mutation; Peptide Hydrolases; Salmonella typhimurium
 +
 +
|- class="tableEdit_footer"
 +
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2871.H4f58f6765de10&page=2871&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||
 +
|}
 +
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.2871.H4f58f6765de10-->
 +
 +
==Main Points of the Paper ==
 +
{{LitSignificance}}
 +
 +
== Materials and Methods Used ==
 +
{{LitMaterials}}
 +
 +
==Phenotype Annotations==
 +
{{AnnotationTableHelp}}
 +
<protect><!--box uid=d41d8cd98f00b204e9800998ecf8427e.2871.K4f58f6766ca19-->
 +
<!--
 +
******************************************************************************************
 +
*
 +
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
 +
*
 +
****************************************************************************************** -->
 +
{|  id="K4f58f6766ca19"  class=" tableEdit Phenotype_Table_2" 
 +
|-
 +
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status
 +
 +
|- class="tableEdit_footer"
 +
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2871.K4f58f6766ca19&page=2871&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table]</span> || || || || || || || || ||
 +
|}
 +
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.2871.K4f58f6766ca19--></protect>
 +
 +
==Notes==
 +
 +
==References==
 +
{{RefHelp}}
 +
<references/>
 +
 +
 +
[[Category:Publication]]

Latest revision as of 13:12, 8 March 2012

Citation

Braun, V, Günthner, K, Hantke, K and Zimmermann, L (1983) Intracellular activation of albomycin in Escherichia coli and Salmonella typhimurium.J. Bacteriol. 156:308-15

Abstract

The antibiotic albomycin is actively taken up by Escherichia coli via the transport system for the structurally similar iron complex ferrichrome. Albomycin is cleaved, and the antibiotically active moiety is released into the cytoplasm, whereas the iron carrier moiety appears in the medium. Besides transport-negative mutants, additional albomycin-resistant mutants were isolated. The mutations were mapped outside the transport genes close to the pyrD gene at 21 min. The mutants were devoid of peptidase N activity. The molecular weight, sensitivity to inhibitors, and cytoplasmic location of the enzyme hydrolyzing albomycin in vitro corresponded to the known properties of peptidase N. The aminoacyl thioribosyl pyrimidine moiety of albomycin apparently has to be cleaved off the iron chelate transport vehicle to inhibit growth. Peptidase N is the major hydrolyzing enzyme. In Salmonella typhimurium peptidase N and peptidase A were equally active in hydrolyzing and activating albomycin.

Links

PubMed

Keywords

Aminopeptidases; Anti-Bacterial Agents; Aspartic Acid Endopeptidases; Biotransformation; Endopeptidases; Escherichia coli; Ferrichrome; Mutation; Peptide Hydrolases; Salmonella typhimurium

edit table

Main Points of the Paper

Please summarize the main points of the paper.

Materials and Methods Used

Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).

Phenotype Annotations

See Help:AnnotationTable for details on how to edit this table.
<protect>

Phenotype of Taxon Information Genotype Information (if known) Condition Information OMP ID OMP Term Name ECO ID ECO Term Name Notes Status
edit table

</protect>

Notes

References

See Help:References for how to manage references in omp dev.

Retrieved from "http://bcbp-ftq4xm2.biobio.tamu.edu/omp/dev/index.php?title=PMID:6352681&oldid=6494"