PMID:372184: Difference between revisions

From EcoliWiki
Jump to navigation Jump to search
/Volumes/r3/t3/ul/working/touchTables/touch_all_tables.php
imported>Wikientrybot
change PMID template to TableEdit version
Line 1: Line 1:
{{RightTOC}}
{{RightTOC}}
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.130844.E522394ddd1035-->
<!--
******************************************************************************************
*
*  ** PLEASE DON'T EDIT THIS TABLE DIRECTLY.  Use the edit table link under the table. **
*
****************************************************************************************** -->
{|  id="E522394ddd1035"  class=" tableEdit PMID_info_table" 


<span style = 'font-size: large'> '''Stayton, MM and Fromm, HJ'''  (1979) Guanosine 5'-diphosphate-3'-diphosphate inhibition of adenylosuccinate synthetase.''J. Biol. Chem.'' '''254''':2579-81</span>
|-
!align=left  |Citation
||
'''No author listed'''  (1979) Guanosine 5'-diphosphate-3'-diphosphate inhibition of adenylosuccinate synthetase. ''J. Biol. Chem.'' '''254''':2579-81
|-
!align=left  |Abstract
||
The mechanism of ppGpp inhibition of adenylosuccinate synthetase (EC 6.3.4.4) was examined. Initial rate kinetic studies demonstrate the ppGpp inhibition is competitive with respect to GTP and noncompetitive with respect to L-aspartate and IMP. This is in contrast to an earlier report (Gallant, J., Irr, J., and Cashel, M. (1971) J. Biol. Chem. 246, 5812-5816), which suggested that ppGpp did not bind at the GTP site. Possible reasons for the discrepancy are discussed. The potency of the ppGpp inhibition is confirmed.
|-
!align=left  |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=372184 PubMed]


{|{{Prettytable}} align = 'center' width= '70%'
|-
|-
|{{TableHeadingColor}} |'''Abstract''' || The mechanism of ppGpp inhibition of adenylosuccinate synthetase (EC 6.3.4.4) was examined. Initial rate kinetic studies demonstrate the ppGpp inhibition is competitive with respect to GTP and noncompetitive with respect to L-aspartate and IMP. This is in contrast to an earlier report (Gallant, J., Irr, J., and Cashel, M. (1971) J. Biol. Chem. 246, 5812-5816), which suggested that ppGpp did not bind at the GTP site. Possible reasons for the discrepancy are discussed. The potency of the ppGpp inhibition is confirmed.
!align=left  |Keywords
</noinclude>
||
|-
Adenylosuccinate Synthase/antagonists & inhibitors; Escherichia coli/enzymology; Guanine Nucleotides/pharmacology; Guanosine Tetraphosphate/pharmacology; Guanosine Triphosphate/pharmacology; Inosine Monophosphate/pharmacology; Kinetics; Ligases/antagonists & inhibitors
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=372184 PubMed]
 
|- class="tableEdit_footer"
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.130844.E522394ddd1035&page=130844&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> ||
|}
|}
 
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.130844.E522394ddd1035-->
==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}

Revision as of 19:26, 1 September 2013

Citation

No author listed (1979) Guanosine 5'-diphosphate-3'-diphosphate inhibition of adenylosuccinate synthetase. J. Biol. Chem. 254:2579-81

Abstract

The mechanism of ppGpp inhibition of adenylosuccinate synthetase (EC 6.3.4.4) was examined. Initial rate kinetic studies demonstrate the ppGpp inhibition is competitive with respect to GTP and noncompetitive with respect to L-aspartate and IMP. This is in contrast to an earlier report (Gallant, J., Irr, J., and Cashel, M. (1971) J. Biol. Chem. 246, 5812-5816), which suggested that ppGpp did not bind at the GTP site. Possible reasons for the discrepancy are discussed. The potency of the ppGpp inhibition is confirmed.

Links

PubMed

Keywords

Adenylosuccinate Synthase/antagonists & inhibitors; Escherichia coli/enzymology; Guanine Nucleotides/pharmacology; Guanosine Tetraphosphate/pharmacology; Guanosine Triphosphate/pharmacology; Inosine Monophosphate/pharmacology; Kinetics; Ligases/antagonists & inhibitors

Significance

You can help EcoliWiki by summarizing why this paper is useful

Useful Materials and Methods

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status

EcoliWiki Links

Add links to pages that link here (e.g. gene, product, method pages)

References

See Help:References for how to manage references in EcoliWiki.